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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]] 4.18&Aring;' scene=''>
<StructureSection load='5xwt' size='340' side='right'caption='[[5xwt]], [[Resolution|resolution]] 4.18&Aring;' 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XWT FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.178&#8491;</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xwt OCA], [http://pdbe.org/5xwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xwt RCSB], [http://www.ebi.ac.uk/pdbsum/5xwt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xwt ProSAT]</span></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=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 ==
[[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> 
[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: Protein-tyrosine-phosphatase]]
[[Category: Homo sapiens]]
[[Category: Fukai, S]]
[[Category: Large Structures]]
[[Category: Goto-Ito, S]]
[[Category: Mus musculus]]
[[Category: Sato, Y]]
[[Category: Fukai S]]
[[Category: Yamagata, A]]
[[Category: Goto-Ito S]]
[[Category: Cell adhesion]]
[[Category: Sato Y]]
[[Category: Synaptic orgnizer]]
[[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

5xwt is a 4 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4.178Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTPRD_MOUSE

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[1]

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

See Also

References

  1. 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:http://dx.doi.org/10.1038/s41467-017-02417-z

5xwt, resolution 4.18Å

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OCA