Pub. Date : 1992 Mar 10
PMID : 1547237
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The global folding of these conformations is similar to that in the thrombin-bound state, as indicated by NOE"s involving the side-chain protons of residues Phe(56), Ile(59), Pro(60), Tyr(63), and Leu(64). | Isoleucine | coagulation factor II, thrombin | Homo sapiens |
| 2 | An analysis of the side-chain rotamers revealed that, upon binding to thrombin, there may be a rotation around the alpha CH-beta CH bond of Ile(59) such that Ile(59) adopts a gauche- (chi 1 = +60) conformation in contrast to the highly populated trans (chi 1 = -60) found for Ile(59) in the free peptide. | Isoleucine | coagulation factor II, thrombin | Homo sapiens |
| 3 | An analysis of the side-chain rotamers revealed that, upon binding to thrombin, there may be a rotation around the alpha CH-beta CH bond of Ile(59) such that Ile(59) adopts a gauche- (chi 1 = +60) conformation in contrast to the highly populated trans (chi 1 = -60) found for Ile(59) in the free peptide. | Isoleucine | coagulation factor II, thrombin | Homo sapiens |
| 4 | An analysis of the side-chain rotamers revealed that, upon binding to thrombin, there may be a rotation around the alpha CH-beta CH bond of Ile(59) such that Ile(59) adopts a gauche- (chi 1 = +60) conformation in contrast to the highly populated trans (chi 1 = -60) found for Ile(59) in the free peptide. | Isoleucine | coagulation factor II, thrombin | Homo sapiens |
| 5 | The apparent preference for a gauche- (chi 1 = +60) side-chain conformation of Ile(59) in the bound state may be explained by the existence of a positively charged arginine residue among the hydrophobic residues in the thrombin exosite. | Isoleucine | coagulation factor II, thrombin | Homo sapiens |