1kjt: Difference between revisions
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[[Image:1kjt.gif|left|200px]] | [[Image:1kjt.gif|left|200px]] | ||
'''Crystal Structure of the GABA(A) Receptor Associated Protein, GABARAP''' | {{Structure | ||
|PDB= 1kjt |SIZE=350|CAPTION= <scene name='initialview01'>1kjt</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure of the GABA(A) Receptor Associated Protein, GABARAP''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KJT is a [ | 1KJT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJT OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the GABA(A)-receptor-associated protein, GABARAP., Bavro VN, Sola M, Bracher A, Kneussel M, Betz H, Weissenhorn W, EMBO Rep. 2002 Feb;3(2):183-9. Epub 2002 Jan 29. PMID:[http:// | Crystal structure of the GABA(A)-receptor-associated protein, GABARAP., Bavro VN, Sola M, Bracher A, Kneussel M, Betz H, Weissenhorn W, EMBO Rep. 2002 Feb;3(2):183-9. Epub 2002 Jan 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11818336 11818336] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ubiquitin-like fold]] | [[Category: ubiquitin-like fold]] | ||
''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 12:18:22 2008'' | ||
Revision as of 13:18, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the GABA(A) Receptor Associated Protein, GABARAP
OverviewOverview
The GABA(A)-receptor-associated protein (GABARAP) is a member of a growing family of intracellular membrane trafficking and/or fusion proteins and has been implicated in plasma membrane targeting and/or recycling of GABA(A) receptors. GABARAP is localized on intracellular membranes such as the trans-Golgi network, binds to the gamma 2 subunit of GABA(A) receptors and interacts with microtubules and the N-ethylmaleimide-sensitive factor. We report the X-ray crystal structure of mammalian GABARAP at 2.0 A resolution. GABARAP consists of an N-terminal basic helical region, which has been implicated in tubulin binding, and a core structure with a conserved ubiquitin-like fold. Consistent with the high extent of sequence conservation among GABARAP homologues from plants to mammals, one face of the core structure is absolutely conserved while the opposite face shows considerable divergence. These features are in agreement with the conserved surface mediating protein-protein interactions shared by all members of the family, whereas the non-conserved surface region may play specific roles, such as docking to particular membrane receptors.
About this StructureAbout this Structure
1KJT is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the GABA(A)-receptor-associated protein, GABARAP., Bavro VN, Sola M, Bracher A, Kneussel M, Betz H, Weissenhorn W, EMBO Rep. 2002 Feb;3(2):183-9. Epub 2002 Jan 29. PMID:11818336
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