2HWL
Crystal structure of thrombin in complex with fibrinogen gamma' peptide
2HWL の概要
| エントリーDOI | 10.2210/pdb2hwl/pdb |
| 分子名称 | Prothrombin, Fibrinogen gamma' peptide, SODIUM ION, ... (6 entities in total) |
| 機能のキーワード | thrombin, fibrinogen, gamma' peptide, serine protease structure, allostery, hydrolase |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| タンパク質・核酸の鎖数 | 5 |
| 化学式量合計 | 69652.03 |
| 構造登録者 | Pineda, A.O.,Chen, Z.W.,Marino, F.,Mathews, F.S.,Mosesson, M.W.,Di Cera, E. (登録日: 2006-08-01, 公開日: 2006-09-19, 最終更新日: 2024-11-06) |
| 主引用文献 | Pineda, A.O.,Chen, Z.W.,Marino, F.,Mathews, F.S.,Mosesson, M.W.,Di Cera, E. Crystal structure of thrombin in complex with fibrinogen gamma' peptide. Biophys.Chem., 125:556-559, 2007 Cited by PubMed Abstract: Elevated levels of heterodimeric gamma(A)/gamma' fibrinogen 2 have been associated with an increased incidence of coronary artery disease, whereas a lowered content of gamma' chains is associated with an increased risk of venous thrombosis. Both situations may be related to the unique features of thrombin binding to variant gamma' chains. The gamma' peptide is an anionic fragment that binds thrombin with high affinity without interfering directly with substrate binding. Here we report the crystal structure of thrombin bound to the gamma' peptide, solved at 2.4 A resolution. The complex reveals extensive interactions between thrombin and the gamma' peptide mediated by electrostatic contacts with residues of exosite II and hydrophobic interactions with a pocket in close proximity to the Na(+) binding site. In its binding mode, the gamma' peptide completely overlaps with heparin bound to exosite II. These findings are consistent with functional data and broaden our understanding of how thrombin interacts with fibrinogen at the molecular level. PubMed: 16962697DOI: 10.1016/j.bpc.2006.08.005 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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