Mechanisms of Macromolecular Protease Inhibitors

被引：95
作者：
Farady, Christopher J. [1 ,2 ]
Craik, Charles S. [1 ,2 ]
机构：
[1] Univ Calif San Francisco, Grad Grp Biophys, San Francisco, CA 94143 USA
[2] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94143 USA
来源：
CHEMBIOCHEM | 2010年 / 11卷 / 17期
基金：
美国国家卫生研究院;
关键词：
inhibitors; mechanisms; proteases; protein engineering; specificity; KUNITZ DOMAIN INHIBITORS; FACTOR-FACTOR VIIA; TRYPSIN-INHIBITOR; MOLECULAR-INTERACTIONS; PLASMINOGEN-ACTIVATOR; STRUCTURAL BASIS; BETA-TRYPSIN; BINDING; CHYMOTRYPSIN; ANTIBODIES;
D O I：
10.1002/cbic.201000442
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Relatively few design principles underlie the inhibition mechanisms of macromolecular protease inhibitors. These inhibitors tend to compete with substrate binding either through direct competition or deformation of the protease active site; they gain potency and specificity by burying a large surface area and through contacts with specific exosites. Protein engineering has allowed both potency and specificity to be modified. Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码：2341 / 2346
页数：6
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