van de Locht A, Stubbs M T, Bauer M, Bode W
Department of Structural Research, Max Planck Institute for Biochemistry, D-82152 Martinsried, Germany.
J Biol Chem. 1996 Feb 16;271(7):3413-6. doi: 10.1074/jbc.271.7.3413.
The 2.6-A x-ray crystal structure of bovine alpha-thrombin in complex with rhodniin, a protein inhibitor isolated from the bug Rhodnius prolixus, has been solved and refined. The structure has enabled us to trace the N-terminal part of the 49-residue A-chain of bovine alpha-thrombin for the first time, which is fixed in a U-shaped loop on the molecular surface opposite the active site canyon. Model building shows that the 25 amino acid residues that link the A-chain and F2 kringle cannot run through the fibrinogen recognition exosite. This demonstrates that this fibrinogen recognition exosite is available in prothrombin and meizothrombin.
已解析并优化了牛α-凝血酶与红猎蝽蛋白抑制剂罗德尼因（rhodniin）复合物的2.6埃X射线晶体结构，该抑制剂是从昆虫长红猎蝽（Rhodnius prolixus）中分离得到的。该结构首次使我们能够追踪牛α-凝血酶49个残基A链的N端部分，其固定在与活性位点峡谷相对的分子表面的一个U形环中。模型构建表明，连接A链和F2 kringle的25个氨基酸残基无法穿过纤维蛋白原识别外位点。这表明该纤维蛋白原识别外位点在凝血酶原和中凝血酶中是存在的。
