View source for 2jsn


==Solution structure of the atypical PDZ-like domain of synbindin==
<StructureSection load='2jsn' size='340' side='right'caption='[[2jsn]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jsn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JSN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2jsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jsn OCA], [https://pdbe.org/2jsn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jsn RCSB], [https://www.ebi.ac.uk/pdbsum/2jsn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jsn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPPC4_HUMAN TPPC4_HUMAN] May play a role in vesicular transport from endoplasmic reticulum to Golgi.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/js/2jsn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2jsn ConSurf].
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== Publication Abstract from PubMed ==
Synbindin is one component of Transport protein particle (TRAPP) complexes. In the hippocampal neurons, synbindin binds syndecan-2 by its atypical PDZ domain (APD) and may regulate the formation of dendritic spines. To investigate the interaction of synbindin and syndecan-2, we determined the solution structure of the synbindin APD by NMR. The structure of APD is different from the classical canonical PDZ domains by lacking the typical alphaA helix and the signature sequence Gly-Psi-Gly-Psi. These differences indicate that APD may not bind syndecan-2 with the typical binding mode of other PDZ domain proteins. In NMR titration experiments, APD do not bind with the C-terminal TKEFYA peptide of syndecan-2, but can interact with the 32-residue cytoplasmic domain of syndecan-2 very weakly.

Solution structure of synbindin atypical PDZ domain and interaction with syndecan-2.,Fan S, Feng Y, Wei Z, Xia B, Gong W Protein Pept Lett. 2009;16(2):189-95. PMID:19200043<ref>PMID:19200043</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2jsn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Fan S]]
[[Category: Feng Y]]
[[Category: Gong W]]
[[Category: Xia B]]