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==Crystal structure of mouse CNTN2 FN1-FN3 domains==
==Crystal structure of mouse CNTN2 FN1-FN3 domains==
<StructureSection load='5e7l' size='340' side='right' caption='[[5e7l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5e7l' size='340' side='right'caption='[[5e7l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5e7l]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E7L FirstGlance]. <br>
<table><tr><td colspan='2'>[[5e7l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E7L FirstGlance]. <br>
</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=5e7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e7l OCA], [http://pdbe.org/5e7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e7l RCSB], [http://www.ebi.ac.uk/pdbsum/5e7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e7l ProSAT]</span></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]] 2.002&#8491;</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=5e7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e7l OCA], [https://pdbe.org/5e7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e7l RCSB], [https://www.ebi.ac.uk/pdbsum/5e7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e7l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CNTN2_MOUSE CNTN2_MOUSE]] In conjunction with another transmembrane protein, CNTNAP2, contributes to the organization of axonal domains at nodes of Ranvier by maintaining voltage-gated potassium channels at the juxtaparanodal region.  
[https://www.uniprot.org/uniprot/CNTN2_MOUSE CNTN2_MOUSE] In conjunction with another transmembrane protein, CNTNAP2, contributes to the organization of axonal domains at nodes of Ranvier by maintaining voltage-gated potassium channels at the juxtaparanodal region.
<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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5e7l" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bouyain, S]]
[[Category: Large Structures]]
[[Category: Nikolaienko, R M]]
[[Category: Mus musculus]]
[[Category: Cell adhesion]]
[[Category: Bouyain S]]
[[Category: Fibronectin type iii domain]]
[[Category: Nikolaienko RM]]
[[Category: Neural cell adhesion molecule]]

Latest revision as of 15:27, 6 March 2024

Crystal structure of mouse CNTN2 FN1-FN3 domainsCrystal structure of mouse CNTN2 FN1-FN3 domains

Structural highlights

5e7l is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.002Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CNTN2_MOUSE In conjunction with another transmembrane protein, CNTNAP2, contributes to the organization of axonal domains at nodes of Ranvier by maintaining voltage-gated potassium channels at the juxtaparanodal region.

5e7l, resolution 2.00Å

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