2ht6: Difference between revisions
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|PDB= 2ht6 |SIZE=350|CAPTION= <scene name='initialview01'>2ht6</scene>, resolution 2.400Å | |PDB= 2ht6 |SIZE=350|CAPTION= <scene name='initialview01'>2ht6</scene>, resolution 2.400Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= GEM, KIR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= GEM, KIR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ht6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ht6 OCA], [http://www.ebi.ac.uk/pdbsum/2ht6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ht6 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Gem, a member of the Rad,Gem/Kir subfamily of small G-proteins, has unique sequence features. We report here the crystallographic structure determination of the Gem G-domain in complex with nucleotide to 2.4 A resolution. Although the basic Ras protein fold is maintained, the Gem switch regions emphatically differ from the Ras paradigm. Our ensuing biochemical characterization indicates that Gem G-domain markedly prefers GDP over GTP. Two known functions of Gem are distinctly affected by spatially separated clusters of mutations. | Gem, a member of the Rad,Gem/Kir subfamily of small G-proteins, has unique sequence features. We report here the crystallographic structure determination of the Gem G-domain in complex with nucleotide to 2.4 A resolution. Although the basic Ras protein fold is maintained, the Gem switch regions emphatically differ from the Ras paradigm. Our ensuing biochemical characterization indicates that Gem G-domain markedly prefers GDP over GTP. Two known functions of Gem are distinctly affected by spatially separated clusters of mutations. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Hirsch, J A.]] | [[Category: Hirsch, J A.]] | ||
[[Category: Opatowsky, Y.]] | [[Category: Opatowsky, Y.]] | ||
[[Category: small g-protein]] | [[Category: small g-protein]] | ||
''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 03:35:03 2008'' | ||
Revision as of 03:35, 31 March 2008
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| , resolution 2.400Å | |||||||
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| Ligands: | , | ||||||
| Gene: | GEM, KIR (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Human Gem G-domain bound to GDP
OverviewOverview
Gem, a member of the Rad,Gem/Kir subfamily of small G-proteins, has unique sequence features. We report here the crystallographic structure determination of the Gem G-domain in complex with nucleotide to 2.4 A resolution. Although the basic Ras protein fold is maintained, the Gem switch regions emphatically differ from the Ras paradigm. Our ensuing biochemical characterization indicates that Gem G-domain markedly prefers GDP over GTP. Two known functions of Gem are distinctly affected by spatially separated clusters of mutations.
About this StructureAbout this Structure
2HT6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure-function studies of the G-domain from human gem, a novel small G-protein., Opatowsky Y, Sasson Y, Shaked I, Ward Y, Chomsky-Hecht O, Litvak Y, Selinger Z, Kelly K, Hirsch JA, FEBS Lett. 2006 Oct 30;580(25):5959-64. Epub 2006 Oct 6. PMID:17052716
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