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==Crystal Structure of the GABA(A) Receptor Associated Protein, GABARAP==
==Crystal Structure of the GABA(A) Receptor Associated Protein, GABARAP==
<StructureSection load='1kjt' size='340' side='right' caption='[[1kjt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1kjt' size='340' side='right'caption='[[1kjt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1kjt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KJT FirstGlance]. <br>
<table><tr><td colspan='2'>[[1kjt]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KJT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kjt OCA], [http://pdbe.org/1kjt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kjt RCSB], [http://www.ebi.ac.uk/pdbsum/1kjt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kjt ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kjt OCA], [https://pdbe.org/1kjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kjt RCSB], [https://www.ebi.ac.uk/pdbsum/1kjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kjt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GBRAP_RAT GBRAP_RAT]] Involved in apoptosis (By similarity). May play a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in autophagy (By similarity).<ref>PMID:11461150</ref>
[https://www.uniprot.org/uniprot/GBRAP_RAT GBRAP_RAT] Involved in apoptosis (By similarity). May play a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in autophagy (By similarity).<ref>PMID:11461150</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kjt ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kjt ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:11818336</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kjt" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[GABA(A) receptor-associated protein|GABA(A) receptor-associated protein]]
*[[GABA receptor-associated protein 3D structures|GABA receptor-associated protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Bavro, V N]]
[[Category: Rattus norvegicus]]
[[Category: Betz, H]]
[[Category: Bavro VN]]
[[Category: Bracher, A]]
[[Category: Betz H]]
[[Category: Kneussel, M]]
[[Category: Bracher A]]
[[Category: Sola, M]]
[[Category: Kneussel M]]
[[Category: Weissenhorn, W]]
[[Category: Sola M]]
[[Category: N-terminal alpha helical region]]
[[Category: Weissenhorn W]]
[[Category: Transport protein]]
[[Category: Ubiquitin-like fold]]

Latest revision as of 10:25, 14 February 2024

Crystal Structure of the GABA(A) Receptor Associated Protein, GABARAPCrystal Structure of the GABA(A) Receptor Associated Protein, GABARAP

Structural highlights

1kjt is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GBRAP_RAT Involved in apoptosis (By similarity). May play a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in autophagy (By similarity).[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Kittler JT, Rostaing P, Schiavo G, Fritschy JM, Olsen R, Triller A, Moss SJ. The subcellular distribution of GABARAP and its ability to interact with NSF suggest a role for this protein in the intracellular transport of GABA(A) receptors. Mol Cell Neurosci. 2001 Jul;18(1):13-25. PMID:11461150 doi:http://dx.doi.org/10.1006/mcne.2001.1005

1kjt, resolution 2.00Å

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