5xnq

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==Crystal structures of human SALM5==
==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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<StructureSection load='5xnq' size='340' side='right'caption='[[5xnq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xnq]] is a 1 chain structure. 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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<table><tr><td colspan='2'>[[5xnq]] is a 1 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=5XNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.802&#8491;</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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xnq OCA], [https://pdbe.org/5xnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xnq RCSB], [https://www.ebi.ac.uk/pdbsum/5xnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xnq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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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[https://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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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5xnq" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lin, Z]]
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[[Category: Homo sapiens]]
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[[Category: Liu, H]]
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[[Category: Large Structures]]
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[[Category: Xu, F]]
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[[Category: Lin Z]]
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[[Category: Membrane protein]]
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[[Category: Liu H]]
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[[Category: Regulating some neural development]]
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[[Category: Xu F]]

Current revision

Crystal structures of human SALM5

PDB ID 5xnq

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