Pleckstrin homology domains: Two halves make a hole?

被引：38

作者：

Lemmon, MA ^{[1
]}

机构：

[1] Univ Penn, Sch Med, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

来源：

CELL | 2005年 / 120卷 / 05期

关键词：

D O I：

10.1016/j.cell.2005.02.023

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：

In a recent issue of Nature, van Rossum et al. report binding of a "split" pleckstrin homology (PH) domain from phospholipase C-gamma(1) to the TRPC3 ion channel. Through sequence analyses and in vitro studies, they suggest a novel mode of protein-protein interaction in which two PH domain fragments in distinct proteins associate to form an "intermolecular" PH domain that binds inositol phospholipids and is required for ion channel location and function.

引用

页码：574 / 576

页数：3

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