2zmv: Difference between revisions

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<StructureSection load='2zmv' size='340' side='right'caption='[[2zmv]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='2zmv' size='340' side='right'caption='[[2zmv]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2zmv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZMV FirstGlance]. <br>
<table><tr><td colspan='2'>[[2zmv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZMV FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRAPPC4, SBDN, CGI-104, HSPC172, PTD009 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.8&#8491;</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=2zmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zmv OCA], [https://pdbe.org/2zmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zmv RCSB], [https://www.ebi.ac.uk/pdbsum/2zmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zmv 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=2zmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zmv OCA], [https://pdbe.org/2zmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zmv RCSB], [https://www.ebi.ac.uk/pdbsum/2zmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zmv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/TPPC4_HUMAN TPPC4_HUMAN]] May play a role in vesicular transport from endoplasmic reticulum to Golgi.  
[https://www.uniprot.org/uniprot/TPPC4_HUMAN TPPC4_HUMAN] May play a role in vesicular transport from endoplasmic reticulum to Golgi.
== 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=2zmv 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=2zmv ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Transport protein particle (TRAPP) is a large multiprotein complex that involves in ER-to-Golgi and intra-Golgi traffic. Synbindin, the human ortholog of yeast Trs23, is one component of the TRAPP complexes. In the hippocampal neurons the synbindin/syndecan complex is involved in synaptic membrane trafficking and thereby regulates the formation of dendritic spines. Here we present the three-dimensional structure of human synbindin, which contains a longin domain (LD) and an atypical PDZ domain (APD). In the crystal, synbindin forms a hexamer, in which the LD forms two different conformations and the APD is quite disordered. These conformational changes of synbindin suggest a possible interaction mode of the LD.
Crystal structure of human synbindin reveals two conformations of longin domain.,Fan S, Wei Z, Xu H, Gong W Biochem Biophys Res Commun. 2009 Jan 16;378(3):338-43. Epub 2008 May 6. PMID:18466758<ref>PMID:18466758</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2zmv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Fan, F]]
[[Category: Fan F]]
[[Category: Endoplasmic reticulum]]
[[Category: Er-golgi transport]]
[[Category: Golgi apparatus]]
[[Category: Longin domain]]
[[Category: Synbindin]]
[[Category: Transport]]
[[Category: Transport protein]]