Phospholipase A(2) - A structural review
Phospholipase A(2) - A structural review
复制标题
DOI：
10.1016/0041-0101(96)00036-0
复制
发表时间：
1996-08-01
期刊：
影响因子：
2.8
通讯作者：
Ward, RJ
中科院分区：
文献类型：
--
作者：
Arni, RK;Ward, RJ
磷脂酶A(2)在自然界中分布广泛，是一种具有催化和药理活性的蛋白质，最近从X射线衍射和核磁共振研究中获得了丰富的结构信息，尽管已经提出了关于磷脂酶A(2)催化机理的详细模型，但解放军(2)其他方面功能的结构基础，如界面激活和毒液，仍存在争议。对聚乳酸(2)蛋白质结构的评价将对这些活动产生新的见解，本文从功能作用方面讨论了I、II和III类聚乳酸(2)的显著结构特征。版权所有(C)1996，爱思唯尔科学有限公司出版
Phospholipases A(2) (PLA(2)) are widely distributed in nature and are well characterized proteins with respect to their catalytic and pharmacological activities, A wealth of structural information has recently become available both from X-ray diffraction and NMR studies, and although a detailed model of the catalytic mechanism of PLA(2) has been proposed, the structural bases of other aspects of PLA(2) function, such as interfacial activation and venom PLA(2) pharmacological activities, are still under debate. An appreciation of the PLA(2) protein structure will yield new insights with regard to these activities, The salient structural features of the class I, II and III PLA(2) are discussed with respect to their functional roles. Copyright (C) 1996 Published by Elsevier Science Ltd