2byf

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[[Image:2byf.gif|left|200px]]
[[Image:2byf.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2byf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2byf OCA], [http://www.ebi.ac.uk/pdbsum/2byf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2byf RCSB]</span>
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'''NMR SOLUTION STRUCTURE OF PHOSPHOLIPASE C EPSILON RA 2 DOMAIN'''
'''NMR SOLUTION STRUCTURE OF PHOSPHOLIPASE C EPSILON RA 2 DOMAIN'''
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[[Category: Rodrigues-Lima, F.]]
[[Category: Rodrigues-Lima, F.]]
[[Category: Roe, S M.]]
[[Category: Roe, S M.]]
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[[Category: lipase]]
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[[Category: Lipase]]
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[[Category: phospholipase c epsilon]]
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[[Category: Phospholipase c epsilon]]
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[[Category: ras binding domain]]
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[[Category: Ras binding domain]]
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[[Category: ubiquitin superfold]]
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[[Category: Ubiquitin superfold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:58:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:13:47 2008''
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Revision as of 17:58, 3 May 2008

Image:2byf.gif

Template:STRUCTURE 2byf

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 Page seeded by OCA on Sat May 3 20:58:09 2008

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