1kjt: Difference between revisions
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<StructureSection load='1kjt' size='340' side='right'caption='[[1kjt]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1kjt' size='340' side='right'caption='[[1kjt]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1kjt]] is a 1 chain structure with sequence from [ | <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'>[ | <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 == | ||
[[ | [[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]] | ||
Revision as of 09:54, 11 August 2021
Crystal Structure of the GABA(A) Receptor Associated Protein, GABARAPCrystal Structure of the GABA(A) Receptor Associated Protein, GABARAP
Structural highlights
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 PubMedThe 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. See AlsoReferences
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