2byf

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Revision as of 06:50, 21 November 2007

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NMR SOLUTION STRUCTURE OF PHOSPHOLIPASE C EPSILON RA 2 DOMAIN

Overview

Ras proteins signal to a number of distinct pathways by interacting with, diverse effectors. Studies of ras/effector interactions have focused on, three classes, Raf kinases, ral guanylnucleotide-exchange factors, and, phosphatidylinositol-3-kinases. Here we describe ras interactions with, another effector, the recently identified phospholipase C epsilon, (PLCepsilon). We solved structures of PLCepsilon RA domains (RA1 and RA2), by NMR and the structure of the RA2/ras complex by X-ray crystallography., Although the similarity between ubiquitin-like folds of RA1 and RA2 proves, that they are homologs, only RA2 can bind ras. Some of the features of the, RA2/ras interface are unique to PLCepsilon, while the ability to make, contacts with both switch I and II regions of ras is shared only with, phosphatidylinositol-3-kinase. Studies of PLCepsilon regulation suggest, that, in a cellular context, the RA2 domain, in a mode specific to, PLCepsilon, has a role in membrane targeting with further regulatory, impact on PLC activity.

About this Structure

2BYF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural and mechanistic insights into ras association domains of phospholipase C epsilon., Bunney TD, Harris R, Gandarillas NL, Josephs MB, Roe SM, Sorli SC, Paterson HF, Rodrigues-Lima F, Esposito D, Ponting CP, Gierschik P, Pearl LH, Driscoll PC, Katan M, Mol Cell. 2006 Feb 17;21(4):495-507. PMID:16483931

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