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1wer
From Proteopedia
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[[Image:1wer.jpg|left|200px]] | [[Image:1wer.jpg|left|200px]] | ||
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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.]] | ||
| - | [[Category: | + | [[Category: Cancer]] |
| - | [[Category: | + | [[Category: Gap]] |
| - | [[Category: | + | [[Category: Growth regulation]] |
| - | [[Category: | + | [[Category: Gtpase activation]] |
| - | [[Category: | + | [[Category: Ra]] |
| - | [[Category: | + | [[Category: Signal transduction]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:33:03 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:33, 3 May 2008
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
