1wer: Difference between revisions
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'''RAS-GTPASE-ACTIVATING DOMAIN OF HUMAN P120GAP''' | {{Structure | ||
|PDB= 1wer |SIZE=350|CAPTION= <scene name='initialview01'>1wer</scene>, resolution 1.60Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= GENE FRAGMENT OF P120GAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''RAS-GTPASE-ACTIVATING DOMAIN OF HUMAN P120GAP''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1WER is a [ | 1WER is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WER OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8955277 8955277] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: growth regulation]] | [[Category: growth regulation]] | ||
[[Category: gtpase activation]] | [[Category: gtpase activation]] | ||
[[Category: | [[Category: ra]] | ||
[[Category: signal transduction]] | [[Category: signal transduction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:56:01 2008'' | ||
Revision as of 12:56, 20 March 2008
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| 1wer, resolution 1.60Å | |||||||||||||
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| Gene: | GENE FRAGMENT OF P120GAP (Homo sapiens) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.
Disease
Known diseases associated with this structure: Basal cell carcinoma, somatic OMIM:[139150], Capillary malformation-arteriovenous malformation OMIM:[139150], Parkes Weber syndrome OMIM:[139150]
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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