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Inhibitor binding to thrombin: x-ray crystallographic studies.

作者信息

Banner D W, Hadváry P

机构信息

Pharmaceutical Research Departments, F. Hoffmann-La Roche Ltd., Basel, Switzerland.

出版信息

Adv Exp Med Biol. 1993;340:27-33. doi: 10.1007/978-1-4899-2418-6_3.

DOI:10.1007/978-1-4899-2418-6_3
PMID:8154341
Abstract
摘要

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Geometry of binding of the benzamidine- and arginine-based inhibitors N alpha-(2-naphthyl-sulphonyl-glycyl)-DL-p-amidinophenylalanyl-pipe ridine (NAPAP) and (2R,4R)-4-methyl-1-[N alpha-(3-methyl-1,2,3,4-tetrahydro-8- quinolinesulphonyl)-L-arginyl]-2-piperidine carboxylic acid (MQPA) to human alpha-thrombin. X-ray crystallographic determination of the NAPAP-trypsin complex and modeling of NAPAP-thrombin and MQPA-thrombin.基于苯甲脒和精氨酸的抑制剂Nα-(2-萘磺酰基-甘氨酰)-DL-对脒基苯丙氨酰哌啶（NAPAP）和(2R,4R)-4-甲基-1-[Nα-(3-甲基-1,2,3,4-四氢-8-喹啉磺酰基)-L-精氨酰]-2-哌啶羧酸（MQPA）与人α-凝血酶结合的几何学。NAPAP-胰蛋白酶复合物的X射线晶体学测定以及NAPAP-凝血酶和MQPA-凝血酶的建模。
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