5e53: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 5e53 is ON HOLD
+==Crystal structure of chicken CNTN1 FN1-FN3 domains==
+<StructureSection load='5e53' size='340' side='right'caption='[[5e53]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.497&#8491;</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='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>
+</table>
+== 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;">
+== Publication Abstract from PubMed ==
+Protein 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.
-Authors: Nikolaienko, R.M., Bouyain, S.
+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<ref>PMID:27539848</ref>
-Description: Crystal structure of chicken CNTN1 FN1-FN3 domains
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Nikolaienko, R.M]]
+<div class="pdbe-citations 5e53" style="background-color:#fffaf0;"></div>
-[[Category: Bouyain, S]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Gallus gallus]]
+[[Category: Large Structures]]
+[[Category: Bouyain S]]
+[[Category: Nikolaienko RM]]