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分泌型磷脂酶A(2)的界面结合：不仅仅是静电作用，色氨酸起主要作用。

Interfacial binding of secreted phospholipases A(2): more than electrostatics and a major role for tryptophan.

作者信息

Gelb M H, Cho W, Wilton D C

机构信息

Departments of Chemistry and Biochemistry, University of Washington, 351700, Seattle, WA 98195, USA.

出版信息

Curr Opin Struct Biol. 1999 Aug;9(4):428-32. doi: 10.1016/S0959-440X(99)80059-1.

DOI:10.1016/S0959-440X(99)80059-1
PMID:10449366
Abstract

Secreted phospholipases A(2) have similar catalytic sites, but vastly different interfacial binding surfaces that modulate their binding affinity for different kinds of phospholipid vesicles by several orders of magnitude. The structure/function principles that dictate both the differential interfacial binding and the physiological function of these enzymes are beginning to be unraveled.

摘要

分泌型磷脂酶A(2)具有相似的催化位点，但界面结合表面却大不相同，这些表面可将它们对不同种类磷脂囊泡的结合亲和力调节几个数量级。决定这些酶的差异界面结合和生理功能的结构/功能原理正开始被揭示。

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