2c5l

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Revision as of 18:46, 29 October 2007

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spinqualitylabelsall models 2c5l, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF PLC EPSILON RAS ASSOCIATION DOMAIN WITH HRAS

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 ... [(full description)]

About this Structure

2C5L is a [Protein complex] structure of sequences from [Homo sapiens] with MG, GTP and GOL as [ligands]. Active as [[1]], with EC number [3.6.5.2]. 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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