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1kjt

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Revision as of 06:54, 11 August 2021

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

Structural highlights

1kjt is a 1 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ Bavro VN, Sola M, Bracher A, Kneussel M, Betz H, Weissenhorn W. Crystal structure of the GABA(A)-receptor-associated protein, GABARAP. EMBO Rep. 2002 Feb;3(2):183-9. Epub 2002 Jan 29. PMID:11818336 doi:10.1093/embo-reports/kvf026

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kjt"

@@ Line 3: / Line 3: @@
 <StructureSection load='1kjt' size='340' side='right'caption='[[1kjt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == 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/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 [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='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'>[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='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>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1kjt

From Proteopedia

Revision as of 06:54, 11 August 2021

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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