PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29283561-8 2018 These results demonstrate that a single-point mutation in the active site pocket of CYP17A1, even when far from the heme, has profound effects on steroidogenic selectivity in androgen biosynthesis. Heme 116-120 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 84-91 30885648-7 2019 Furthermore, the docking results of 13a revealed that the oxygen atom at the position of C-3 connected to the heme of CYP17, which may be helpful for its satisfactory dual-target inhibition. Heme 110-114 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 118-123 29718108-8 2018 This in silico study showed that LAM was able to bind directly to the heme iron in the active site of CYP17A1, but not CYP21A2, thus supporting the results of the in vitro studies. Heme 70-74 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 102-109 27566228-5 2017 While both hydroxylase and lyase substrates have similar orientations with respect to the heme, subtle differences in hydrogen bonding between CYP17A1 and the C3 substituent at the opposite end of ligands appear to correlate with differential substrate utilization and product formation. Heme 90-94 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 143-150 28373265-2 2017 The steroid abiraterone, the active form of the only CYP17A1 inhibitor approved by the Food and Drug Administration, binds the catalytic heme iron, nonselectively impeding both reactions and ultimately causing undesirable corticosteroid imbalance. Heme 137-141 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 53-60 28373265-5 2017 Binding studies and X-ray structures of CYP17A1 with nonsteroidal inhibitors reveal coordination to the heme iron like the steroidal inhibitors. Heme 104-108 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 40-47 27002602-8 2016 Docking indicated that the N-containing rings of OME possibly could interact with the iron atom of the heme for S-OME in CYP17A1 and S- and R-OME in CYP21A2. Heme 103-107 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 121-128 11243732-8 2001 The proline residue probably causes a turn in the meander region of P450c17, and we hypothesize, by comparison to homologous proteins, that the change in the protein conformation may abolish heme incorporation or may prevent P450c17 from interacting with electron donors. Heme 191-195 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 68-75 19454579-11 2009 Computer-based three-dimensional model analysis of CYP17A1 using CYP2B4 as template showed that three of the mutations had no direct effect on the active center, whereas one affects the heme coordination. Heme 186-190 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 51-58 25650406-10 2015 CONCLUSIONS: p.W121R substitution, affecting the first residue in the conserved heme-interacting WXXXR motif of CYP17A1, is associated with partial combined deficiency of 17alpha-hydroxylase/17,20-lyase. Heme 80-84 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 112-119 24971814-5 2014 Docking of aforementioned compounds to CYP17A1 revealed that steroid fragments of compound 1 and abiraterone 3 occupied close positions; oxazoline cycle of compound 1 was coordinated with heme iron similarly to pyridine cycle of abiraterone 3. Heme 188-192 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 39-46 24328388-0 2014 Resonance Raman spectroscopy reveals that substrate structure selectively impacts the heme-bound diatomic ligands of CYP17. Heme 86-90 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 117-122 21446712-3 2011 Therefore, we hypothesized that the binding of P4 and 17OHP4 to CYP21A2 restricts access of the reactive heme-oxygen complex to the C-21 hydrogen atoms, suppressing oxygenation at kinetically more favorable sites such as C-17 and C-16, which are both hydroxylated by cytochrome P450c17 (CYP17A1). Heme 105-109 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 278-285 21446712-3 2011 Therefore, we hypothesized that the binding of P4 and 17OHP4 to CYP21A2 restricts access of the reactive heme-oxygen complex to the C-21 hydrogen atoms, suppressing oxygenation at kinetically more favorable sites such as C-17 and C-16, which are both hydroxylated by cytochrome P450c17 (CYP17A1). Heme 105-109 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 287-294 16176874-10 2005 In addition, three-dimensional computerized modeling of the heme-binding site of the P450c17 enzyme indicated that replacement of Arg by Cys at amino acid position 440 predicts a loss of the catalytic activity of the enzyme, as the mutant enzyme containing Cys440 fails to form a hydrogen bond with the propionate group of heme, which renders the mutant enzyme unable to stabilize the proper position of heme. Heme 60-64 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 85-92 16176874-10 2005 In addition, three-dimensional computerized modeling of the heme-binding site of the P450c17 enzyme indicated that replacement of Arg by Cys at amino acid position 440 predicts a loss of the catalytic activity of the enzyme, as the mutant enzyme containing Cys440 fails to form a hydrogen bond with the propionate group of heme, which renders the mutant enzyme unable to stabilize the proper position of heme. Heme 323-327 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 85-92 16176874-10 2005 In addition, three-dimensional computerized modeling of the heme-binding site of the P450c17 enzyme indicated that replacement of Arg by Cys at amino acid position 440 predicts a loss of the catalytic activity of the enzyme, as the mutant enzyme containing Cys440 fails to form a hydrogen bond with the propionate group of heme, which renders the mutant enzyme unable to stabilize the proper position of heme. Heme 323-327 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 85-92 16176874-11 2005 Based on these findings we conclude that expressing the CYP17 gene with functional analysis, combined with three-dimensional computerized modeling of the heme-binding site of the protein provide feasible tools for molecular characterizing of functional consequences of the novel CYP17 mutation on enzyme function. Heme 154-158 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 56-61 16176874-11 2005 Based on these findings we conclude that expressing the CYP17 gene with functional analysis, combined with three-dimensional computerized modeling of the heme-binding site of the protein provide feasible tools for molecular characterizing of functional consequences of the novel CYP17 mutation on enzyme function. Heme 154-158 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 279-284 12773039-6 2003 A model that permits hydrogen bond interaction between the azole functionality on ring D and the enzyme is consistent with experimental deductions for type II CYP17 inhibitors where a sixth ligating atom interacts with Fe(II) of heme. Heme 229-233 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 159-164 22217842-7 1992 Based on the results obtained so far we can predict that those 17alpha-hydroxylase deficient individuals having a homozygous stop codon in the CYP17 gene positioned at the amino terminal side of the P450c17 heme-binding cysteine (442) will all have the same phenotype. Heme 207-211 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 143-148 9703423-10 1998 This 1-bp deletion produces a frameshift in translation and introduces a premature stop codon (TAG) proximal to the highly conserved heme iron-binding cysteine at codon 442 in microsomal cytochrome P450 steroid 17alpha-hydroxylase (P450c17). Heme 133-137 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 232-239 9177409-4 1997 This exon skipping alters the translational reading frame of exon 8 and introduces a premature stop codon (TAA) at amino acid position 410 proximal to the heme iron-binding site essential for the enzymatic activity of CYP17. Heme 155-159 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 218-223 22217842-7 1992 Based on the results obtained so far we can predict that those 17alpha-hydroxylase deficient individuals having a homozygous stop codon in the CYP17 gene positioned at the amino terminal side of the P450c17 heme-binding cysteine (442) will all have the same phenotype. Heme 207-211 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 199-206