PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24692562-0 2014 Intramolecular interactions that induce helical rearrangement upon rhodopsin activation: light-induced structural changes in metarhodopsin IIa probed by cysteine S-H stretching vibrations. Cysteine 153-161 rhodopsin Homo sapiens 67-76 28536260-6 2017 Using visual arrestin-1 and rhodopsin as a model, we found that substitution of these cysteines with serine, alanine, or valine virtually eliminates the effects of the activating polar core mutations on the binding to unphosphorylated rhodopsin while only slightly reducing the effects of the C-tail mutations. Cysteine 86-95 rhodopsin Homo sapiens 28-37 28536260-6 2017 Using visual arrestin-1 and rhodopsin as a model, we found that substitution of these cysteines with serine, alanine, or valine virtually eliminates the effects of the activating polar core mutations on the binding to unphosphorylated rhodopsin while only slightly reducing the effects of the C-tail mutations. Cysteine 86-95 rhodopsin Homo sapiens 235-244 3192520-13 1988 Derivatization of Gt alpha at either Cys-210 or Cys-347 by 125I-ACTP inhibited rhodopsin-catalyzed guanosine 5"-3-O-(thio)triphosphate binding to Gt, mimicking the effect of ADP-ribosylation of Cys-347 by pertussis toxin. Cysteine 37-40 rhodopsin Homo sapiens 79-88 3192520-13 1988 Derivatization of Gt alpha at either Cys-210 or Cys-347 by 125I-ACTP inhibited rhodopsin-catalyzed guanosine 5"-3-O-(thio)triphosphate binding to Gt, mimicking the effect of ADP-ribosylation of Cys-347 by pertussis toxin. Cysteine 48-51 rhodopsin Homo sapiens 79-88 3192520-13 1988 Derivatization of Gt alpha at either Cys-210 or Cys-347 by 125I-ACTP inhibited rhodopsin-catalyzed guanosine 5"-3-O-(thio)triphosphate binding to Gt, mimicking the effect of ADP-ribosylation of Cys-347 by pertussis toxin. Cysteine 48-51 rhodopsin Homo sapiens 79-88 24692562-2 2014 To investigate the mechanism by which rhodopsin adopts the transducin-activating conformation, the local environmental changes in the transmembrane region were probed using the cysteine S-H group, whose stretching frequency is well isolated from the other protein vibrational modes. Cysteine 177-185 rhodopsin Homo sapiens 38-47 22842041-1 2012 We have determined the spatial arrangement of rhodopsin in the retinal rod outer segment (ROS) membrane by measuring the distances between rhodopsin molecules in which native cysteines were spin-labeled at ~1.0 mol/mol rhodopsin. Cysteine 175-184 rhodopsin Homo sapiens 46-55 24724832-6 2014 We mapped these sites using a novel tryptophan-induced quenching method, in which we introduced Trp residues into arrestin and measured their ability to quench the fluorescence of bimane probes attached to cysteine residues on TM6 of rhodopsin (T242C and T243C). Cysteine 206-214 rhodopsin Homo sapiens 234-243 27493492-5 2014 The cysteine residues were individually introduced into 15 positions of Helix III, which contains several key amino acid residues for the light-induced conformational changes of rhodopsin. Cysteine 4-12 rhodopsin Homo sapiens 178-187 24106275-4 2013 As a complementary approach, we superimposed this panel of ADRP mutants onto a rhodopsin background containing a juxtaposed cysteine pair (N2C/D282C) that forms a disulfide bond. Cysteine 124-132 rhodopsin Homo sapiens 79-88 22352709-2 2012 To probe the intradimeric proximity of helix 8 (H8), we conducted chemical cross-linking of endogenous cysteines in rhodopsin in disk membranes. Cysteine 103-112 rhodopsin Homo sapiens 116-125 12359230-0 2002 Retinitis pigmentosa-associated rhodopsin mutations in three membrane-located cysteine residues present three different biochemical phenotypes. Cysteine 78-86 rhodopsin Homo sapiens 32-41 17014882-2 2006 Metarhodopsin-II is stabilized when the N-terminus of the carboxyl (340-350) tail peptide of the alpha-subunit of transducin (Gtalpha) is crosslinked to rhodopsin cysteine 140 or the 340-350 peptide C-terminus of Gtalpha is crosslinked to rhodopsin cysteine 316. Cysteine 163-171 rhodopsin Homo sapiens 4-13 17014882-2 2006 Metarhodopsin-II is stabilized when the N-terminus of the carboxyl (340-350) tail peptide of the alpha-subunit of transducin (Gtalpha) is crosslinked to rhodopsin cysteine 140 or the 340-350 peptide C-terminus of Gtalpha is crosslinked to rhodopsin cysteine 316. Cysteine 163-171 rhodopsin Homo sapiens 153-162 17014882-2 2006 Metarhodopsin-II is stabilized when the N-terminus of the carboxyl (340-350) tail peptide of the alpha-subunit of transducin (Gtalpha) is crosslinked to rhodopsin cysteine 140 or the 340-350 peptide C-terminus of Gtalpha is crosslinked to rhodopsin cysteine 316. Cysteine 249-257 rhodopsin Homo sapiens 4-13 15840841-0 2005 Cysteine 2.59(89) in the second transmembrane domain of human CB2 receptor is accessible within the ligand binding crevice: evidence for possible CB2 deviation from a rhodopsin template. Cysteine 0-8 rhodopsin Homo sapiens 167-176 14744159-9 2004 This result indicates that the distances between the phosphorylated sites on the C-terminus and the (19)F sites on helix 8 (Cys 316) and in the second cytoplasmic loop (Cys140) are greater than 12 A in phosphorylated rhodopsin. Cysteine 124-127 rhodopsin Homo sapiens 217-226 12590586-1 2003 This report describes the biochemical characterization of a double mutant of rhodopsin (N2C,D282C) in which Cys residues engineered into the protein at positions 2 (in the amino-terminal extracellular domain) and 282 (in the extracellular loop between transmembrane helices 6 and 7) are shown to form a disulfide bond and increase the thermal stability of the unliganded or opsin form of the protein. Cysteine 108-111 rhodopsin Homo sapiens 77-86 19934058-2 2009 When the corresponding cysteine is mutated in rhodopsin, it disrupts proper folding of the pigment, causing severe, early onset retinitis pigmentosa. Cysteine 23-31 rhodopsin Homo sapiens 46-55 18067244-3 2008 The new thiol-active reagents were labeled cytoplasmic cysteine 140 and 316 in rhodopsin (Rh), a G protein coupled receptor (GPCR). Cysteine 55-63 rhodopsin Homo sapiens 79-88 18067244-3 2008 The new thiol-active reagents were labeled cytoplasmic cysteine 140 and 316 in rhodopsin (Rh), a G protein coupled receptor (GPCR). Cysteine 55-63 rhodopsin Homo sapiens 90-92 17009319-6 2006 The model is found to correctly predict 93% of the experimentally observed effects in 119 rhodopsin mutants for which the decay rates and misfolding data have been measured, including a systematic analysis of Cys-->Ser replacements reported here. Cysteine 209-212 rhodopsin Homo sapiens 90-99 11697851-0 2001 Chemical modification of transducin with iodoacetic acid: transducin-alpha carboxymethylated at Cys(347) allows transducin binding to Light-activated rhodopsin but prevents its release in the presence of GTP. Cysteine 96-99 rhodopsin Homo sapiens 150-159 12081478-1 2002 The crystal structure of rhodopsin revealed a cytoplasmic helical segment (H8) extending from transmembrane (TM) helix seven to a pair of vicinal palmitoylated cysteine residues. Cysteine 160-168 rhodopsin Homo sapiens 25-34 12065750-4 2002 The different amino acid sequence that forms helix 3 in rhodopsin (basically the conserved Gly(3.36)Glu(3.37) motif in the opsin family) and the 5-HT1A receptor (the conserved Cys(3.36)Thr(3.37) motif in the neurotransmitter family) produces these structural divergences. Cysteine 176-179 rhodopsin Homo sapiens 56-65 11866527-0 2002 X-ray diffraction of heavy-atom labelled two-dimensional crystals of rhodopsin identifies the position of cysteine 140 in helix 3 and cysteine 316 in helix 8. Cysteine 106-114 rhodopsin Homo sapiens 69-78 11866527-0 2002 X-ray diffraction of heavy-atom labelled two-dimensional crystals of rhodopsin identifies the position of cysteine 140 in helix 3 and cysteine 316 in helix 8. Cysteine 134-142 rhodopsin Homo sapiens 69-78 11601970-0 2001 Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1. Cysteine 194-203 rhodopsin Homo sapiens 71-80 11601971-0 2001 Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between cysteine pairs engineered in cytoplasmic loops 1, 3, and 4. Cysteine 172-180 rhodopsin Homo sapiens 71-80 11106502-2 2000 Rhodopsin in native membranes was selectively modified with fluorescent Alexa594-maleimide at the Cys(316) position, with a large excess of the reagent Cys(140) that was also derivatized. Cysteine 98-101 rhodopsin Homo sapiens 0-9 11408595-3 2001 Moreover, the amino acid residues inferred to form the surface of the binding-site crevice based on our application of the substituted-cysteine accessibility method in the dopamine D(2) receptor are in remarkable agreement with the rhodopsin structure, with the notable exception of some residues in the fourth transmembrane segment. Cysteine 135-143 rhodopsin Homo sapiens 232-241 11320236-2 2001 Previous work has shown that misfolding is caused by the formation of a disulfide bond in the ID domain different from the native Cys-110-Cys-187 disulfide bond in native rhodopsin. Cysteine 130-133 rhodopsin Homo sapiens 171-180 11320236-2 2001 Previous work has shown that misfolding is caused by the formation of a disulfide bond in the ID domain different from the native Cys-110-Cys-187 disulfide bond in native rhodopsin. Cysteine 138-141 rhodopsin Homo sapiens 171-180 11320237-6 2001 Crosslinking was demonstrated between T and a number of single cysteine rhodopsin mutants. Cysteine 63-71 rhodopsin Homo sapiens 72-81 11106502-2 2000 Rhodopsin in native membranes was selectively modified with fluorescent Alexa594-maleimide at the Cys(316) position, with a large excess of the reagent Cys(140) that was also derivatized. Cysteine 152-155 rhodopsin Homo sapiens 0-9 10570143-2 1999 Single cysteine substitution mutants in the cytoplasmic face of rhodopsin were labeled by attachment of the trifluoroethylthio (TET), CF(3)-CH(2)-S, group through a disulfide linkage. Cysteine 7-15 rhodopsin Homo sapiens 64-73 10570143-3 1999 TET-labeled cysteine mutants at amino acid positions 67, 140, 245, 248, 311, and 316 in rhodopsin were thus prepared. Cysteine 12-20 rhodopsin Homo sapiens 88-97 10051572-0 1999 Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function. Cysteine 88-97 rhodopsin Homo sapiens 26-35 10387035-1 1999 Sixteen single-cysteine substitution mutants of rhodopsin were prepared in the sequence 306-321 which begins in transmembrane helix VII and ends at the palmitoylation sites at 322C and 323C. Cysteine 15-23 rhodopsin Homo sapiens 48-57 10387036-0 1999 Single-cysteine substitution mutants at amino acid positions 55-75, the sequence connecting the cytoplasmic ends of helices I and II in rhodopsin: reactivity of the sulfhydryl groups and their derivatives identifies a tertiary structure that changes upon light-activation. Cysteine 7-15 rhodopsin Homo sapiens 136-145 10387036-1 1999 Cysteines were introduced, one at a time, at amino acid positions 55-75 in the cytoplasmic region connecting helices I and II in rhodopsin. Cysteine 0-9 rhodopsin Homo sapiens 129-138 10508406-3 1999 In this study, we utilized this method to examine the cross-linking reactions between native cysteines in the ground state and after photoexcitation of rhodopsin. Cysteine 93-102 rhodopsin Homo sapiens 152-161 10508407-1 1999 Previous studies [Yu, H., Kono, M., and Oprian, D. D. (1999) Biochemistry 38, xxxx-xxxx] using split receptors and disulfide cross-linking have shown that native cysteines 140 and 222 on the cytoplasmic side of transmembrane segments (TM) 3 and 5 of rhodopsin, respectively, can cross-link to each other upon treatment with the oxidant Cu(phen)3(2+). Cysteine 162-171 rhodopsin Homo sapiens 250-259 10051572-0 1999 Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function. Cysteine 88-97 rhodopsin Homo sapiens 127-136 10051572-0 1999 Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function. Cysteine 99-102 rhodopsin Homo sapiens 26-35 10051572-0 1999 Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function. Cysteine 99-102 rhodopsin Homo sapiens 127-136 10051572-1 1999 The disulfide bond between Cys-110 and Cys-187 in the intradiscal domain is required for correct folding in vivo and function of mammalian rhodopsin. Cysteine 27-30 rhodopsin Homo sapiens 139-148 10051572-1 1999 The disulfide bond between Cys-110 and Cys-187 in the intradiscal domain is required for correct folding in vivo and function of mammalian rhodopsin. Cysteine 39-42 rhodopsin Homo sapiens 139-148 9477956-1 1998 Rhodopsin contains two cysteines (Cys110 and Cys187) that are highly conserved among members of the G protein coupled receptor family and that form a disulfide bond connecting helixes 3 and 4 on the extracellular side of the protein. Cysteine 23-32 rhodopsin Homo sapiens 0-9 9880548-3 1999 We investigated this hypothesis using a series of eight rhodopsin mutants containing single reactive cysteine residues in the region (helix F) where movement was previously detected. Cysteine 101-109 rhodopsin Homo sapiens 56-65 9797678-0 1998 Ocular signs associated with a rhodopsin mutation (Cys-167-->Arg) in a family with autosomal dominant retinitis pigmentosa. Cysteine 51-54 rhodopsin Homo sapiens 31-40 8823930-1 1996 The location of cysteines accessible in octopus rhodopsin were characterized by a spin-labeling technique. Cysteine 16-25 rhodopsin Homo sapiens 48-57 8864113-2 1996 Such changes in rhodopsin were explored by construction of double cysteine mutants, each containing one cysteine at the cytoplasmic end of helix C and one cysteine at various positions in the cytoplasmic end of helix F. Magnetic dipolar interactions between spin labels attached to these residues revealed their proximity, and changes in their interaction upon rhodopsin light activation suggested a rigid body movement of helices relative to one another. Cysteine 66-74 rhodopsin Homo sapiens 16-25 9405601-1 1997 Cysteine mutagenesis and site-directed spin labeling in the C-terminal region of rhodopsin have been used to probe the local structure and proximity of that region to the cytoplasmic loops. Cysteine 0-8 rhodopsin Homo sapiens 81-90 8052635-1 1994 We prepared rhodopsin mutants that contained a single reactive cysteine residue per rhodopsin molecule at position 65, 140, 240, or 316 on the cytoplasmic face. Cysteine 63-71 rhodopsin Homo sapiens 12-21 7612621-5 1995 All of the cysteine substitution mutants formed the characteristic rhodopsin chromophore (lambda max, 500 nm) with 11-cis-retinal. Cysteine 11-19 rhodopsin Homo sapiens 67-76 7612621-10 1995 These findings highlight intrinsic differences in both the reactivity and accessibility of the different cysteine residues in the CD loop and support the important role for a structure in the second cytoplasmic region of rhodopsin. Cysteine 105-113 rhodopsin Homo sapiens 221-230 7972030-2 1994 This cysteine is known to be palmitoylated in rhodopsin, the beta 2-adrenergic receptor (beta 2AR) and the alpha 2A-adrenergic receptor (alpha 2AAR). Cysteine 5-13 rhodopsin Homo sapiens 46-55 8052635-1 1994 We prepared rhodopsin mutants that contained a single reactive cysteine residue per rhodopsin molecule at position 65, 140, 240, or 316 on the cytoplasmic face. Cysteine 63-71 rhodopsin Homo sapiens 84-93 8052635-2 1994 A carbene-generating photoactivatable group was linked by a disulfide bond to the cysteine sulfhydryl group of each of the rhodopsin mutants. Cysteine 82-90 rhodopsin Homo sapiens 123-132 8052635-4 1994 Subsequent photoactivation (355 nm) of the carbene-generating group resulted in crosslinking of the rhodopsin mutant carrying a cysteine residue at position 240 to transducin. Cysteine 128-136 rhodopsin Homo sapiens 100-109 8218279-1 1993 Five mutations of rhodopsin have been produced, each of which contains a unique cysteine residue at positions 62, 65, 140, 240, or 316 in the cytoplasmic domain. Cysteine 80-88 rhodopsin Homo sapiens 18-27 8075342-0 1994 Photoactivation of rhodopsin involves alterations in cysteine side chains: detection of an S-H band in the Meta I-->Meta II FTIR difference spectrum. Cysteine 53-61 rhodopsin Homo sapiens 19-28 8075342-1 1994 FTIR difference spectroscopy has been used to study the role of cysteine residues in the photoactivation of rhodopsin. Cysteine 64-72 rhodopsin Homo sapiens 108-117 8075342-2 1994 A positive band near 2550 cm-1 with a low frequency shoulder is detected during rhodopsin photobleaching, which is assigned on the basis of its frequency and isotope shift to the S-H stretching mode of one or more cysteine residues. Cysteine 214-222 rhodopsin Homo sapiens 80-89 8075342-6 1994 On this basis, it is likely that at least one of the four remaining cysteine residues in rhodopsin is structurally active during rhodopsin photoactivation. Cysteine 68-76 rhodopsin Homo sapiens 89-98 8075342-6 1994 On this basis, it is likely that at least one of the four remaining cysteine residues in rhodopsin is structurally active during rhodopsin photoactivation. Cysteine 68-76 rhodopsin Homo sapiens 129-138 8171030-0 1994 Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state. Cysteine 63-71 rhodopsin Homo sapiens 26-35 8171030-0 1994 Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state. Cysteine 63-71 rhodopsin Homo sapiens 138-147 8171030-1 1994 A disulfide bond that is evidently conserved in the guanine nucleotide-binding protein-coupled receptors is present in rhodopsin between Cys-110 and Cys-187. Cysteine 137-140 rhodopsin Homo sapiens 119-128 8171030-1 1994 A disulfide bond that is evidently conserved in the guanine nucleotide-binding protein-coupled receptors is present in rhodopsin between Cys-110 and Cys-187. Cysteine 149-152 rhodopsin Homo sapiens 119-128 8171030-2 1994 We have replaced these two cysteine residues by alanine residues and now report on the properties of the resulting rhodopsin mutants. Cysteine 27-35 rhodopsin Homo sapiens 115-124 8469290-3 1993 A wealth of biochemical data is available for rhodopsin: 11-cis retinal is bound to lysine 296 in helix VII; glutamic acid 113 on helix III is the counterion to the protonated Schiff"s base; a disulphide bridge, cystine 110-187, connects helix III to the second extracellular loop e2 (refs 13, 14); the carboxy terminus has two palmitoylated cysteines forming a cytoplasmic loop i4 (ref. Cysteine 342-351 rhodopsin Homo sapiens 46-55