5e53: Difference between revisions
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<StructureSection load='5e53' size='340' side='right'caption='[[5e53]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='5e53' size='340' side='right'caption='[[5e53]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5e53]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5e53]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E53 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]] 2.497Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5e53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e53 OCA], [https://pdbe.org/5e53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e53 RCSB], [https://www.ebi.ac.uk/pdbsum/5e53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e53 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CNTN1_CHICK CNTN1_CHICK] Mediates cell surface interactions during nervous system development. Interaction with TNR enhances the neurite outgrowth.<ref>PMID:7615642</ref> | ||
<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 5e53" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5e53" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bouyain | [[Category: Bouyain S]] | ||
[[Category: Nikolaienko | [[Category: Nikolaienko RM]] | ||
Latest revision as of 09:13, 5 July 2023
Crystal structure of chicken CNTN1 FN1-FN3 domainsCrystal structure of chicken CNTN1 FN1-FN3 domains
Structural highlights
FunctionCNTN1_CHICK Mediates cell surface interactions during nervous system development. Interaction with TNR enhances the neurite outgrowth.[1] Publication Abstract from PubMedProtein tyrosine phosphatase receptor type G (RPTPgamma/PTPRG) interacts in vitro with contactin-3-6 (CNTN3-6), a group of glycosylphosphatidyl-anchored cell adhesion molecules involved in the wiring of the nervous system. In addition to PTPRG, CNTNs associate with multiple transmembrane proteins and signal inside the cell via cis-binding partners to alleviate the absence of an intracellular region. Here, we use comprehensive biochemical and structural analyses to demonstrate that PTPRG[middot]CNTN3-6 complexes share similar binding affinities and a conserved arrangement. Furthermore, as a first step to identifying PTPRG.CNTN complexes in vivo, we found that PTPRG and CNTN3 associate in the outer segments of mouse rod photoreceptor cells. In particular, PTPRG and CNTN3 form cis-complexes at the surface of photoreceptors, yet interact in trans when expressed on the surfaces of apposing cells. Further structural analyses suggest that all CNTN ectodomains adopt a bent conformation and might lie parallel to the cell surface to accommodate these cis and trans binding modes. Taken together, these studies identify a PTPRG.CNTN complex in vivo and provide novel insights into PTPRG- and CNTN- mediated signaling. Structural Basis for Interactions Between Contactin Family Members and Protein Tyrosine Phosphatase Receptor Type G in Neural Tissues.,Nikolaienko RM, Hammel M, Dubreuil V, Zalmai R, Hall DR, Mehzabeen N, Karuppan SJ, Harroch S, Stella SL, Bouyain S J Biol Chem. 2016 Aug 18. pii: jbc.M116.742163. PMID:27539848[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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