The BON domain: a putative membrane-binding domain

被引：70

作者：

Yeats, C ^{[1
]}

Bateman, A ^{[1
]}

机构：

[1] Wellcome Trust Sanger Inst, Hinxton CB10 1SA, England

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2003年 / 28卷 / 07期

关键词：

D O I：

10.1016/S0968-0004(03)00115-4

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：

A novel conserved protein region - the BON (bacterial OsmY and nodulation) domain - is found in the bacterial osmotic-shock-resistance protein OsmY, a family of haemolysins, a group of nodulation specificity proteins and secretory channels, and several hypothetical proteins. Functional annotation in the literature suggests that it interacts with phospholipid membranes. A lack of catalytic residues in the sequence alignment supports the hypothesis that it is a binding domain.

引用

页码：352 / 355

页数：4

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