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普列克底物蛋白同源结构域:具有多种功能的常见折叠结构。

Pleckstrin homology domains: a common fold with diverse functions.

作者信息

Rebecchi M J, Scarlata S

机构信息

Department of Anesthesiology, State University of New York at Stony Brook 11794, USA.

出版信息

Annu Rev Biophys Biomol Struct. 1998;27:503-28. doi: 10.1146/annurev.biophys.27.1.503.

DOI:10.1146/annurev.biophys.27.1.503
PMID:9646876
Abstract

Pleckstrin homology (PH) motifs are approximately 100 amino-acid residues long and have been identified in nearly 100 different eukaryotic proteins, many of which participate in cell signaling and cytoskeletal regulation. Despite minimal sequence homology, the three-dimensional structures are remarkably conserved. This review gives an overview of the PH domain architecture and examines the best-studied examples in an attempt to understand their function.

摘要

普列克底物蛋白同源(PH)基序约含100个氨基酸残基,已在近100种不同的真核生物蛋白质中被鉴定出来,其中许多蛋白质参与细胞信号传导和细胞骨架调节。尽管序列同源性很低,但三维结构却非常保守。本综述概述了PH结构域的结构,并研究了一些研究得较为透彻的例子,以期了解它们的功能。

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