2bmj: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmj OCA], [http://www.ebi.ac.uk/pdbsum/2bmj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bmj RCSB]</span> | |||
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[[Category: structural genomics consortium]] | [[Category: structural genomics consortium]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:08:36 2008'' | ||
Revision as of 23:08, 30 March 2008
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| 2bmj, resolution 2.10Å | |||||||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
GTPASE LIKE DOMAIN OF CENTAURIN GAMMA 1 (HUMAN)
Overview
Centaurins are a family of proteins that contain GTPase-activating protein domains, with the gamma family members containing in addition a GTPase-like domain. Centaurins reside mainly in the nucleus and are known to activate phosphoinositide 3-kinase, a key regulator of cell proliferation, motility and vesicular trafficking. In the present study, using X-ray structural analysis, enzymatic assays and nucleotide-binding studies, we show that, for CENTG1 (centaurin gamma-1) the GTPase-like domain has broader trinucleotide specificity. Alterations within the G4 motif of CENTG1 from the highly conserved NKXD found in typical GTPases to TQDR result in the loss of specificity, a lower affinity for the nucleotides and higher turnover rates. These results indicate that the centaurins could be more accurately classified as NTPases and point to alternative mechanisms of cell signalling control.
About this Structure
2BMJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The centaurin gamma-1 GTPase-like domain functions as an NTPase., Soundararajan M, Yang X, Elkins JM, Sobott F, Doyle DA, Biochem J. 2007 Feb 1;401(3):679-88. PMID:17037982
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