View source for 5xpv


==Structure of the V domain of amphioxus IgVJ-C2==
<StructureSection load='5xpv' size='340' side='right'caption='[[5xpv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xpv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Branchiostoma_floridae Branchiostoma floridae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XPV 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]] 1.9&#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=5xpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xpv OCA], [https://pdbe.org/5xpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xpv RCSB], [https://www.ebi.ac.uk/pdbsum/5xpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xpv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C3ZN36_BRAFL C3ZN36_BRAFL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The emergence of adaptive immunity in jawed vertebrates depended on the appearance of variable immune receptors, BCRs and TCRs, which exhibit variable-J-constant (VJ-C)-type Ig superfamily folds. Hitherto, however, the structures of IgV-J-IgC-type molecules had never been characterized in invertebrates, leaving the origin of BCR/TCR-type molecules unknown. Using x-ray crystallography, the structure of a VJ-C2 molecule, named AmpIgVJ-C2, was determined in amphioxus (Branchiostoma floridae). The first domain shows typical V folding, including the hydrophobic core, CDR analogs, and eight conserved residues. The second domain is a C2-type Ig superfamily domain, as defined by its short length and the absence of beta-strand D- and C1-typical motifs. AmpIgVJ-C2 molecules form homodimers, using "three-layer packing dimerization," as described for TCRs and BCRs. The AmpIgVJ-C2 V domain harbors a diglycine motif in beta-strand G and forms a beta-bulge structure participating in V-V intermolecular interaction. By immunohistochemistry, AmpIgVJ-C2 molecules were primarily found in mucosal tissues, whereas PCR and sequence analysis indicated considerable genetic variation at the single-gene level; these findings would be consistent with an immune function and a basic ability to adapt to binding different immune targets. Our results show a BCR/TCR-ancestral like molecule in amphioxus and help us to understand the evolution of the adaptive immune system.

Discovery and Analysis of Invertebrate IgVJ-C2 Structure from Amphioxus Provides Insight into the Evolution of the Ig Superfamily.,Chen R, Zhang L, Qi J, Zhang N, Zhang L, Yao S, Wu Y, Jiang B, Wang Z, Yuan H, Zhang Q, Xia C J Immunol. 2018 Apr 15;200(8):2869-2881. doi: 10.4049/jimmunol.1700906. Epub 2018, Mar 7. PMID:29514951<ref>PMID:29514951</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xpv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Branchiostoma floridae]]
[[Category: Large Structures]]
[[Category: Chen R]]
[[Category: Jiang B]]
[[Category: Qi J]]
[[Category: Wang Z]]
[[Category: Wu Y]]
[[Category: Xia C]]
[[Category: Yao S]]
[[Category: Yuan H]]
[[Category: Zhang L]]
[[Category: Zhang N]]
[[Category: Zhang Q]]