1rgp

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{{STRUCTURE_1rgp| PDB=1rgp | SCENE= }}
{{STRUCTURE_1rgp| PDB=1rgp | SCENE= }}
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'''GTPASE-ACTIVATION DOMAIN FROM RHOGAP'''
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===GTPASE-ACTIVATION DOMAIN FROM RHOGAP===
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==Overview==
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Members of the Rho family of small G proteins transduce signals from plasma-membrane receptors and control cell adhesion, motility and shape by actin cytoskeleton formation. They also activate other kinase cascades. Like all other GTPases, Rho proteins act as molecular switches, with an active GTP-bound form and an inactive GDP-bound form. The active conformation is promoted by guanine-nucleotide exchange factors, and the inactive state by GTPase-activating proteins (GAPs) which stimulate the intrinsic GTPase activity of small G proteins. Rho-specific GAP domains are found in a wide variety of large, multi-functional proteins. Here we report the crystal structure of an active 242-residue C-terminal fragment of human p50rhoGAP. The structure is an unusual arrangement of nine alpha-helices, the core of which includes a four-helix bundle. Residues conserved across the rhoGAP family are largely confined to one face of this bundle, which may be an interaction site for target G proteins. In particular, we propose that Arg 85 and Asn 194 are involved in binding G proteins and enhancing GTPase activity.
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(as it appears on PubMed at http://www.pubmed.gov), where 9009196 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9009196}}
==About this Structure==
==About this Structure==
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[[Category: Gap]]
[[Category: Gap]]
[[Category: Signal-transduction]]
[[Category: Signal-transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:28:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:18:10 2008''

Revision as of 09:18, 29 July 2008

Image:1rgp.png

Template:STRUCTURE 1rgp

GTPASE-ACTIVATION DOMAIN FROM RHOGAP

Template:ABSTRACT PUBMED 9009196

About this Structure

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

Reference

The structure of the GTPase-activating domain from p50rhoGAP., Barrett T, Xiao B, Dodson EJ, Dodson G, Ludbrook SB, Nurmahomed K, Gamblin SJ, Musacchio A, Smerdon SJ, Eccleston JF, Nature. 1997 Jan 30;385(6615):458-61. PMID:9009196

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