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1wer

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{{STRUCTURE_1wer| PDB=1wer | SCENE= }}
{{STRUCTURE_1wer| PDB=1wer | SCENE= }}
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'''RAS-GTPASE-ACTIVATING DOMAIN OF HUMAN P120GAP'''
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===RAS-GTPASE-ACTIVATING DOMAIN OF HUMAN P120GAP===
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==Overview==
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Ras-related GTP-binding proteins function as molecular switches which cycle between GTP-bound 'on'- and GDP-bound 'off'-states. GTP hydrolysis is the common timing mechanism that mediates the return from the 'on' to the 'off'-state. It is usually slow but can be accelerated by orders of magnitude upon interaction with GTPase-activating proteins (GAPs). In the case of Ras, a major regulator of cellular growth, point mutations are found in approximately 30% of human tumours which render the protein unable to hydrolyse GTP, even in the presence of Ras-GAPs. The first structure determination of a GTPase-activating protein reveals the catalytically active fragment of the Ras-specific p120GAP (ref. 2), GAP-334, as an elongated, exclusively helical protein which appears to represent a novel protein fold. The molecule consists of two domains, one of which contains all the residues conserved among different GAPs for Ras. From the location of conserved residues around a shallow groove in the central domain we can identify the site of interaction with Ras x GTP. This leads to a model for the interaction between Ras and GAP that satisfies numerous biochemical and genetic data on this important regulatory process.
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{{ABSTRACT_PUBMED_8955277}}
==About this Structure==
==About this Structure==
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[[Category: Ra]]
[[Category: Ra]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:15:10 2008''

Revision as of 13:15, 28 July 2008

Image:1wer.png

Template:STRUCTURE 1wer

RAS-GTPASE-ACTIVATING DOMAIN OF HUMAN P120GAP

Template:ABSTRACT PUBMED 8955277

About this Structure

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

Reference

Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras., Scheffzek K, Lautwein A, Kabsch W, Ahmadian MR, Wittinghofer A, Nature. 1996 Dec 12;384(6609):591-6. PMID:8955277

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