1wer

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[[Image:1wer.jpg|left|200px]]
[[Image:1wer.jpg|left|200px]]
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{{Structure
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|PDB= 1wer |SIZE=350|CAPTION= <scene name='initialview01'>1wer</scene>, resolution 1.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1wer", creates the "Structure Box" on the page.
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|GENE= GENE FRAGMENT OF P120GAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1wer| PDB=1wer | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wer OCA], [http://www.ebi.ac.uk/pdbsum/1wer PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wer RCSB]</span>
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'''RAS-GTPASE-ACTIVATING DOMAIN OF HUMAN P120GAP'''
'''RAS-GTPASE-ACTIVATING DOMAIN OF HUMAN P120GAP'''
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[[Category: Scheffzek, K.]]
[[Category: Scheffzek, K.]]
[[Category: Wittinghofer, A.]]
[[Category: Wittinghofer, A.]]
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[[Category: cancer]]
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[[Category: Cancer]]
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[[Category: gap]]
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[[Category: Gap]]
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[[Category: growth regulation]]
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[[Category: Growth regulation]]
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[[Category: gtpase activation]]
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[[Category: Gtpase activation]]
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[[Category: ra]]
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[[Category: Ra]]
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[[Category: signal transduction]]
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[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:33:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:35:15 2008''
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Revision as of 10:33, 3 May 2008

Template:STRUCTURE 1wer

RAS-GTPASE-ACTIVATING DOMAIN OF HUMAN P120GAP


Overview

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.

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 Page seeded by OCA on Sat May 3 13:33:03 2008

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