View source for 4pbx


==Crystal structure of the six N-terminal domains of human receptor protein tyrosine phosphatase sigma==
<StructureSection load='4pbx' size='340' side='right'caption='[[4pbx]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pbx]] 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=4PBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PBX 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]] 3.15&#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=4pbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pbx OCA], [https://pdbe.org/4pbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pbx RCSB], [https://www.ebi.ac.uk/pdbsum/4pbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pbx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PTPRS_HUMAN PTPRS_HUMAN] Interacts with LAR-interacting protein LIP.1.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Receptor protein tyrosine phosphatase sigma (RPTPsigma) regulates neuronal extension and acts as a presynaptic nexus for multiple protein and proteoglycan interactions during synaptogenesis. Unknown mechanisms govern the shift in RPTPsigma function, from outgrowth promotion to synaptic organization. Here, we report crystallographic, electron microscopic and small-angle X-ray scattering analyses, which reveal sufficient inter-domain flexibility in the RPTPsigma extracellular region for interaction with both cis (same cell) and trans (opposite cell) ligands. Crystal structures of RPTPsigma bound to its postsynaptic ligand TrkC detail an interaction surface partially overlapping the glycosaminoglycan-binding site. Accordingly, heparan sulphate and heparin oligomers compete with TrkC for RPTPsigma binding in vitro and disrupt TrkC-dependent synaptic differentiation in neuronal co-culture assays. We propose that transient RPTPsigma ectodomain emergence from the presynaptic proteoglycan layer allows capture by TrkC to form a trans-synaptic complex, the consequent reduction in RPTPsigma flexibility potentiating interactions with additional ligands to orchestrate excitatory synapse formation.

Structural basis for extracellular cis and trans RPTPsigma signal competition in synaptogenesis.,Coles CH, Mitakidis N, Zhang P, Elegheert J, Lu W, Stoker AW, Nakagawa T, Craig AM, Jones EY, Aricescu AR Nat Commun. 2014 Nov 11;5:5209. doi: 10.1038/ncomms6209. PMID:25385546<ref>PMID:25385546</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pbx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Aricescu AR]]
[[Category: Coles CH]]
[[Category: Craig AM]]
[[Category: Elegheert J]]
[[Category: Jones EY]]
[[Category: Lu W]]
[[Category: Mitakidis N]]
[[Category: Nakagawa T]]
[[Category: Stoker AW]]
[[Category: Zhang P]]