PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1542664-1 1992 Recent work has suggested that the thrombin-bound conformation of fibrinopeptide A exhibits a strand-turn-strand motif, with a beta-turn centered at residues Glu-11 and Gly-12. Glycine 169-172 coagulation factor II, thrombin Bos taurus 35-43 8400548-1 1993 Previous studies have shown that exogenous glycosphingolipids (GSLs) inhibit the adhesion of thrombin-activated platelets (TAP) to polystyrene plates coated with various RGD-ligands (where RGD is the peptide sequence Arg-Gly-Asp), suggesting that GSLs can modulate the platelet integrin receptor glycoprotein IIb-IIIa. Glycine 221-224 coagulation factor II, thrombin Bos taurus 93-101 7190836-3 1980 The rates of hydrolysis of the Arg-Gly bond in these peptides by thrombin were measured, and the values of the specificity constant, kcat/KM, were all found to be approximately 2 X 10(-7) [(NIH unit/L)s]-1, similar to that for a peptide (F-3) having an additional Arg residue between Glu- and -NHCH3 of F-4. Glycine 35-38 coagulation factor II, thrombin Bos taurus 65-73 7190836-6 1980 The active site of thrombin thus appears to interact with a peptide of the size of F-6, with the Phe residue possibly being in close spatial proximity to the Val-Arg-Gly moiety. Glycine 166-169 coagulation factor II, thrombin Bos taurus 19-27 7370278-5 1980 Thrombin and Factor Xa may possess a hydrophobic region near the P2 binding site which is unfavourable for either asparagine or D-alanine but which readily accommodates glycine, L-alanine or L-phenylalanine. Glycine 169-176 coagulation factor II, thrombin Bos taurus 0-8 9307032-8 1997 There is continuous density for the five residues in the P3, P2, P1, P1" and P2" positions of the peptide (Gly-14f to Pro-18f) at the active site of thrombin, and isolated but well-defined density for Tyr-8f at position P9 in the hydrophobic pocket of thrombin. Glycine 107-110 coagulation factor II, thrombin Bos taurus 149-157 9307032-8 1997 There is continuous density for the five residues in the P3, P2, P1, P1" and P2" positions of the peptide (Gly-14f to Pro-18f) at the active site of thrombin, and isolated but well-defined density for Tyr-8f at position P9 in the hydrophobic pocket of thrombin. Glycine 107-110 coagulation factor II, thrombin Bos taurus 252-260 8855938-1 1996 The crystal structure of the noncovalent complex of bovine thrombin and a fibrinogen-A alpha tridecapeptide substrate analog, G17 psi, in which the scissile bond amide nitrogen of Gly-17f has been replaced by a methylene carbon, has been determined at 2.3 A resolution with an R factor of 17.1%. Glycine 180-183 coagulation factor II, thrombin Bos taurus 59-67 2026264-4 1991 The P1" subsite of P79 is isosteric with the glycine residue of the natural thrombin substrate fibrinogen, but is proteolytically stable due to the incorporation of a ketomethylene pseudopeptide bond. Glycine 45-52 coagulation factor II, thrombin Bos taurus 76-84