1kjt: Difference between revisions

Revision as of 14:34, 21 February 2008

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 with and as ligands. 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

Page seeded by OCA on Thu Feb 21 13:34:52 2008

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OCA

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-[[Image:1kjt.gif|left|200px]]<br /><applet load="1kjt" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1kjt, resolution 2.0&Aring;" />
 '''Crystal Structure of the GABA(A) Receptor Associated Protein, GABARAP'''<br />
 ==Overview==
-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.
+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 Structure==
-KJT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NI and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KJT OCA].
+KJT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJT OCA].
 ==Reference==
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 [[Category: Rattus norvegicus]]
 [[Category: Single protein]]
-[[Category: Bavro, V.N.]]
+[[Category: Bavro, V N.]]
 [[Category: Betz, H.]]
 [[Category: Bracher, A.]]
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 [[Category: ubiquitin-like fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:17:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:52 2008''