1t3e
From Proteopedia
(Difference between revisions)
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<StructureSection load='1t3e' size='340' side='right'caption='[[1t3e]], [[Resolution|resolution]] 3.25Å' scene=''> | <StructureSection load='1t3e' size='340' side='right'caption='[[1t3e]], [[Resolution|resolution]] 3.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1t3e]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1t3e]] is a 3 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=1T3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T3E FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.25Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1t3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t3e OCA], [https://pdbe.org/1t3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t3e RCSB], [https://www.ebi.ac.uk/pdbsum/1t3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t3e ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/GEPH_RAT GEPH_RAT] Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.<ref>PMID:8264797</ref> <ref>PMID:9990024</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=1t3e 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=1t3e ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Gephyrin is a bi-functional modular protein involved in molybdenum cofactor biosynthesis and in postsynaptic clustering of inhibitory glycine receptors (GlyRs). Here, we show that full-length gephyrin is a trimer and that its proteolysis in vitro causes the spontaneous dimerization of its C-terminal region (gephyrin-E), which binds a GlyR beta-subunit-derived peptide with high and low affinity. The crystal structure of the tetra-domain gephyrin-E in complex with the beta-peptide bound to domain IV indicates how membrane-embedded GlyRs may interact with subsynaptic gephyrin. In vitro, trimeric full-length gephyrin forms a network upon lowering the pH, and this process can be reversed to produce stable full-length dimeric gephyrin. Our data suggest a mechanism by which induced conformational transitions of trimeric gephyrin may generate a reversible postsynaptic scaffold for GlyR recruitment, which allows for dynamic receptor movement in and out of postsynaptic GlyR clusters, and thus for synaptic plasticity. | ||
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| - | Structural basis of dynamic glycine receptor clustering by gephyrin.,Sola M, Bavro VN, Timmins J, Franz T, Ricard-Blum S, Schoehn G, Ruigrok RW, Paarmann I, Saiyed T, O'Sullivan GA, Schmitt B, Betz H, Weissenhorn W EMBO J. 2004 Jul 7;23(13):2510-9. Epub 2004 Jun 17. PMID:15201864<ref>PMID:15201864</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1t3e" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Buffalo rat]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bavro | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Franz | + | [[Category: Bavro VN]] |
| - | [[Category: Paarmann | + | [[Category: Franz T]] |
| - | [[Category: Ricard-Blum | + | [[Category: O'Sullivan GA]] |
| - | [[Category: Ruigrok | + | [[Category: Paarmann I]] |
| - | [[Category: Saiyed | + | [[Category: Ricard-Blum S]] |
| - | [[Category: Schoehn | + | [[Category: Ruigrok RWH]] |
| - | [[Category: Sola | + | [[Category: Saiyed T]] |
| - | + | [[Category: Schoehn G]] | |
| - | [[Category: Timmins | + | [[Category: Sola M]] |
| - | + | [[Category: Timmins J]] | |
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Current revision
Structural basis of dynamic glycine receptor clustering
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Categories: Large Structures | Rattus norvegicus | Bavro VN | Franz T | O'Sullivan GA | Paarmann I | Ricard-Blum S | Ruigrok RWH | Saiyed T | Schoehn G | Sola M | Timmins J
