1xx0

From Proteopedia

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Structure of the C-terminal PH domain of human pleckstrin

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Pleckstrin is the major target of protein kinase C (PKC) in blood, platelets. Its phosphorylation triggers responses that ultimately lead to, platelet activation and blood clot formation. Pleckstrin consists of three, domains: a pleckstrin homology (PH) domain at both termini and a central, DEP (Dishevelled, Egl-1, Pleckstrin) domain. Here, we report the solution, nuclear magnetic resonance (NMR) structure of the C-terminal PH domain, (C-PH) of human pleckstrin-1. We show that this PH domain binds, phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4)P2) with high, specificity in protein lipid overlay assays. Using NMR titration, experiments and mutational analysis, residues involved in binding to, PtdIns(3,4)P2 are identified. The binding site is formed by a patch of, basic residues from the beta1 and beta2 strands and the beta1-beta2 loop., Since PtdIns(3,4)P2 is an important signaling molecule in platelets, our, data suggest a C-PH dependent regulation of pleckstrin function in, response to PtdIns(3,4)P2.

Disease

Known disease associated with this structure: Age-related maculopathy, susceptibility to OMIM:[607772]

About this Structure

1XX0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure and phosphatidylinositol-(3,4)-bisphosphate binding of the C-terminal PH domain of human pleckstrin., Edlich C, Stier G, Simon B, Sattler M, Muhle-Goll C, Structure. 2005 Feb;13(2):277-86. PMID:15698571

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