5xws: Difference between revisions

Latest revision as of 12:20, 6 November 2024

Crystal structure of SALM5 LRR-Ig

Structural highlights

5xws is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.084Å
Ligands:	NAG
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

Synapse formation is triggered by trans-synaptic interactions of cell adhesion molecules, termed synaptic organizers. Three members of type-II receptor protein tyrosine phosphatases (classified as type-IIa RPTPs; PTPdelta, PTPsigma and LAR) are known as presynaptic organizers. Synaptic adhesion-like molecules (SALMs) have recently emerged as a family of postsynaptic organizers. Although all five SALM isoforms can bind to the type-IIa RPTPs, only SALM3 and SALM5 reportedly have synaptogenic activities depending on their binding. Here, we report the crystal structures of apo-SALM5, and PTPdelta-SALM2 and PTPdelta-SALM5 complexes. The leucine-rich repeat (LRR) domains of SALMs interact with the second immunoglobulin-like (Ig) domain of PTPdelta, whereas the Ig domains of SALMs interact with both the second and third Ig domains of PTPdelta. Unexpectedly, the structures exhibit the LRR-mediated 2:2 complex. Our synaptogenic co-culture assay using site-directed SALM5 mutants demonstrates that presynaptic differentiation induced by PTPdelta-SALM5 requires the dimeric property of SALM5.

Structural basis of trans-synaptic interactions between PTPdelta and SALMs for inducing synapse formation.,Goto-Ito S, Yamagata A, Sato Y, Uemura T, Shiroshima T, Maeda A, Imai A, Mori H, Yoshida T, Fukai S Nat Commun. 2018 Jan 18;9(1):269. doi: 10.1038/s41467-017-02417-z. PMID:29348429^[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:https://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:https://dx.doi.org/10.1016/j.mcn.2008.05.019
↑ Goto-Ito S, Yamagata A, Sato Y, Uemura T, Shiroshima T, Maeda A, Imai A, Mori H, Yoshida T, Fukai S. Structural basis of trans-synaptic interactions between PTPdelta and SALMs for inducing synapse formation. Nat Commun. 2018 Jan 18;9(1):269. doi: 10.1038/s41467-017-02417-z. PMID:29348429 doi:https://dx.doi.org/10.1038/s41467-017-02417-z

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OCA

[1] 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:https://dx.doi.org/10.1074/jbc.M709456200

[2] 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:https://dx.doi.org/10.1016/j.mcn.2008.05.019

[3] Goto-Ito S, Yamagata A, Sato Y, Uemura T, Shiroshima T, Maeda A, Imai A, Mori H, Yoshida T, Fukai S. Structural basis of trans-synaptic interactions between PTPdelta and SALMs for inducing synapse formation. Nat Commun. 2018 Jan 18;9(1):269. doi: 10.1038/s41467-017-02417-z. PMID:29348429 doi:https://dx.doi.org/10.1038/s41467-017-02417-z

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5xws is ON HOLD  until Paper Publication
+==Crystal structure of SALM5 LRR-Ig==
+<StructureSection load='5xws' size='340' side='right'caption='[[5xws]], [[Resolution|resolution]] 3.08&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5xws]] 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=5XWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XWS FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.084&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=5xws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xws OCA], [https://pdbe.org/5xws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xws RCSB], [https://www.ebi.ac.uk/pdbsum/5xws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xws ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Synapse formation is triggered by trans-synaptic interactions of cell adhesion molecules, termed synaptic organizers. Three members of type-II receptor protein tyrosine phosphatases (classified as type-IIa RPTPs; PTPdelta, PTPsigma and LAR) are known as presynaptic organizers. Synaptic adhesion-like molecules (SALMs) have recently emerged as a family of postsynaptic organizers. Although all five SALM isoforms can bind to the type-IIa RPTPs, only SALM3 and SALM5 reportedly have synaptogenic activities depending on their binding. Here, we report the crystal structures of apo-SALM5, and PTPdelta-SALM2 and PTPdelta-SALM5 complexes. The leucine-rich repeat (LRR) domains of SALMs interact with the second immunoglobulin-like (Ig) domain of PTPdelta, whereas the Ig domains of SALMs interact with both the second and third Ig domains of PTPdelta. Unexpectedly, the structures exhibit the LRR-mediated 2:2 complex. Our synaptogenic co-culture assay using site-directed SALM5 mutants demonstrates that presynaptic differentiation induced by PTPdelta-SALM5 requires the dimeric property of SALM5.
-Authors:
+Structural basis of trans-synaptic interactions between PTPdelta and SALMs for inducing synapse formation.,Goto-Ito S, Yamagata A, Sato Y, Uemura T, Shiroshima T, Maeda A, Imai A, Mori H, Yoshida T, Fukai S Nat Commun. 2018 Jan 18;9(1):269. doi: 10.1038/s41467-017-02417-z. PMID:29348429<ref>PMID:29348429</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5xws" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Fukai S]]
+[[Category: Goto-Ito S]]
+[[Category: Sato Y]]
+[[Category: Yamagata A]]

5xws: Difference between revisions

Latest revision as of 12:20, 6 November 2024

Crystal structure of SALM5 LRR-Ig

Structural highlights

Function

Publication Abstract from PubMed

References

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