5xnp

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(Difference between revisions)

Revision as of 06:46, 7 February 2018

Crystal structures of human SALM5 in complex with human PTPdelta

Structural highlights

5xnp is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Gene:	LRFN5, C14orf146, SALM5 (HUMAN), PTPRD (HUMAN)
Activity:	Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LRFN5_HUMAN] Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons.^[1] ^[2]

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Seabold GK, Wang PY, Chang K, Wang CY, Wang YX, Petralia RS, Wenthold RJ. The SALM family of adhesion-like molecules forms heteromeric and homomeric complexes. J Biol Chem. 2008 Mar 28;283(13):8395-405. doi: 10.1074/jbc.M709456200. Epub 2008, Jan 28. PMID:18227064 doi:http://dx.doi.org/10.1074/jbc.M709456200
↑ Wang PY, Seabold GK, Wenthold RJ. Synaptic adhesion-like molecules (SALMs) promote neurite outgrowth. Mol Cell Neurosci. 2008 Sep;39(1):83-94. doi: 10.1016/j.mcn.2008.05.019. Epub, 2008 Jun 7. PMID:18585462 doi:http://dx.doi.org/10.1016/j.mcn.2008.05.019
↑ Lin Z, Liu J, Ding H, Xu F, Liu H. Structural basis of SALM5-induced PTPdelta dimerization for synaptic differentiation. Nat Commun. 2018 Jan 18;9(1):268. doi: 10.1038/s41467-017-02414-2. PMID:29348579 doi:http://dx.doi.org/10.1038/s41467-017-02414-2

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5xnp"

@@ Line 3: / Line 3: @@
 <StructureSection load='5xnp' size='340' side='right' caption='[[5xnp]], [[Resolution|resolution]] 3.73&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5xnp]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XNP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XNP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5xnp]] is a 4 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=5XNP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XNP FirstGlance]. <br>
 </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>
+<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]), PTPRD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>
 <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=5xnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xnp OCA], [http://pdbe.org/5xnp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xnp RCSB], [http://www.ebi.ac.uk/pdbsum/5xnp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xnp ProSAT]</span></td></tr>
@@ Line 10: / Line 11: @@
 == Function ==
 [[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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5xnp" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Protein-tyrosine-phosphatase]]
 [[Category: Lin, Z]]

5xnp

From Proteopedia

Revision as of 06:46, 7 February 2018

Crystal structures of human SALM5 in complex with human PTPdelta

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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