5xwt: Difference between revisions
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==Crystal structure of PTPdelta Ig1-Fn1 in complex with SALM5 LRR-Ig== | ==Crystal structure of PTPdelta Ig1-Fn1 in complex with SALM5 LRR-Ig== | ||
<StructureSection load='5xwt' size='340' side='right' caption='[[5xwt]], [[Resolution|resolution]] 4.18Å' scene=''> | <StructureSection load='5xwt' size='340' side='right'caption='[[5xwt]], [[Resolution|resolution]] 4.18Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5xwt]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XWT OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5xwt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XWT FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.178Å</td></tr> | ||
<tr id=' | <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>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xwt OCA], [https://pdbe.org/5xwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xwt RCSB], [https://www.ebi.ac.uk/pdbsum/5xwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xwt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PTPRD_MOUSE PTPRD_MOUSE] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5xwt" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5xwt" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tubulin tyrosine ligase 3D structures|Tubulin tyrosine ligase 3D structures]] | |||
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: | [[Category: Fukai S]] | ||
[[Category: | [[Category: Goto-Ito S]] | ||
[[Category: | [[Category: Sato Y]] | ||
[[Category: | [[Category: Yamagata A]] |
Latest revision as of 10:45, 17 October 2024
Crystal structure of PTPdelta Ig1-Fn1 in complex with SALM5 LRR-IgCrystal structure of PTPdelta Ig1-Fn1 in complex with SALM5 LRR-Ig
Structural highlights
FunctionPublication Abstract from PubMedSynapse 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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