1k5d: Difference between revisions
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[[Image:1k5d.gif|left|200px]] | [[Image:1k5d.gif|left|200px]] | ||
'''Crystal structure of Ran-GPPNHP-RanBP1-RanGAP complex''' | {{Structure | ||
|PDB= 1k5d |SIZE=350|CAPTION= <scene name='initialview01'>1k5d</scene>, resolution 2.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of Ran-GPPNHP-RanBP1-RanGAP complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1K5D is a [ | 1K5D is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K5D OCA]. | ||
==Reference== | ==Reference== | ||
RanGAP mediates GTP hydrolysis without an arginine finger., Seewald MJ, Korner C, Wittinghofer A, Vetter IR, Nature. 2002 Feb 7;415(6872):662-6. PMID:[http:// | RanGAP mediates GTP hydrolysis without an arginine finger., Seewald MJ, Korner C, Wittinghofer A, Vetter IR, Nature. 2002 Feb 7;415(6872):662-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11832950 11832950] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[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 12:12:55 2008'' | ||
Revision as of 13:12, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Ran-GPPNHP-RanBP1-RanGAP complex
OverviewOverview
GTPase-activating proteins (GAPs) increase the rate of GTP hydrolysis on guanine nucleotide-binding proteins by many orders of magnitude. Studies with Ras and Rho have elucidated the mechanism of GAP action by showing that their catalytic machinery is both stabilized by GAP binding and complemented by the insertion of a so-called 'arginine finger' into the phosphate-binding pocket. This has been proposed as a universal mechanism for GAP-mediated GTP hydrolysis. Ran is a nuclear Ras-related protein that regulates both transport between the nucleus and cytoplasm during interphase, and formation of the mitotic spindle and/or nuclear envelope in dividing cells. Ran-GTP is hydrolysed by the combined action of Ran-binding proteins (RanBPs) and RanGAP. Here we present the three-dimensional structure of a Ran-RanBP1-RanGAP ternary complex in the ground state and in a transition-state mimic. The structure and biochemical experiments show that RanGAP does not act through an arginine finger, that the basic machinery for fast GTP hydrolysis is provided exclusively by Ran and that correct positioning of the catalytic glutamine is essential for catalysis.
DiseaseDisease
Known diseases associated with this structure: Osteolysis, familial expansile OMIM:[603499], Paget disease of bone OMIM:[603499]
About this StructureAbout this Structure
1K5D is a Protein complex structure of sequences from Homo sapiens and Schizosaccharomyces pombe. Full crystallographic information is available from OCA.
ReferenceReference
RanGAP mediates GTP hydrolysis without an arginine finger., Seewald MJ, Korner C, Wittinghofer A, Vetter IR, Nature. 2002 Feb 7;415(6872):662-6. PMID:11832950
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