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5xnq

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'''Unreleased structure'''
 
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The entry 5xnq is ON HOLD until Paper Publication
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==Crystal structures of human SALM5==
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<StructureSection load='5xnq' size='340' side='right' caption='[[5xnq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5xnq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XNQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XNQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LRFN5, C14orf146, SALM5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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=5xnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xnq OCA], [http://pdbe.org/5xnq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xnq RCSB], [http://www.ebi.ac.uk/pdbsum/5xnq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xnq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/LRFN5_HUMAN LRFN5_HUMAN]] Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons.<ref>PMID:18227064</ref> <ref>PMID:18585462</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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SALM5, a synaptic adhesion molecule implicated in autism, induces presynaptic differentiation through binding to the LAR family receptor protein tyrosine phosphatases (LAR-RPTPs) that have been highlighted as presynaptic hubs for synapse formation. The mechanisms underlying SALM5/LAR-RPTP interaction remain unsolved. Here we report crystal structures of human SALM5 LRR-Ig alone and in complex with human PTPdelta Ig1-3 (MeA(-)). Distinct from other LAR-RPTP ligands, SALM5 mainly exists as a dimer with LRR domains from two protomers packed in an antiparallel fashion. In the 2:2 heterotetrameric SALM5/PTPdelta complex, a SALM5 dimer bridges two separate PTPdelta molecules. Structure-guided mutations and heterologous synapse formation assays demonstrate that dimerization of SALM5 is prerequisite for its functionality in inducing synaptic differentiation. This study presents a structural template for the SALM family and reveals a mechanism for how a synaptic adhesion molecule directly induces cis-dimerization of LAR-RPTPs into higher-order signaling assembly.
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Authors: Liu, H., Lin, Z., Xu, F.
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Structural basis of SALM5-induced PTPdelta dimerization for synaptic differentiation.,Lin Z, Liu J, Ding H, Xu F, Liu H Nat Commun. 2018 Jan 18;9(1):268. doi: 10.1038/s41467-017-02414-2. PMID:29348579<ref>PMID:29348579</ref>
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Description: A novel synaptic protein
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5xnq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Human]]
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[[Category: Lin, Z]]
[[Category: Liu, H]]
[[Category: Liu, H]]
[[Category: Xu, F]]
[[Category: Xu, F]]
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[[Category: Lin, Z]]
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[[Category: Membrane protein]]
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[[Category: Regulating some neural development]]

Current revision

Crystal structures of human SALM5

5xnq, resolution 2.80Å

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