Interfacial binding of secreted phospholipases A2:: more than electrostatics and a major pole for tryptophan

被引：114
作者：
Gelb, MH
Cho, WH
Wilton, DC
机构：
[1] Univ Washington, Dept Chem, Seattle, WA 98195 USA
[2] Univ Washington, Dept Biochem, Seattle, WA 98195 USA
[3] Univ Illinois, Dept Chem MC 111, Chicago, IL 60607 USA
[4] Univ Southampton, Sch Biol Sci, Div Biochem & Mol Biol, Southampton SO16 7PX, Hants, England
来源：
CURRENT OPINION IN STRUCTURAL BIOLOGY | 1999年 / 9卷 / 04期
基金：
英国惠康基金;
关键词：
D O I：
10.1016/S0959-440X(99)80059-1
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：
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.
引用
收藏
页码：428 / 432
页数：5
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