4dfi: Difference between revisions

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New page: '''Unreleased structure''' The entry 4dfi is ON HOLD Authors: Liu, J., Qian, X., Chen, Z., Xu, X., Gao, F., Zhang, S., Zhang, R., Qi, J., Gao, G.F., Yan, J. Description: Crystal struct...
 
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'''Unreleased structure'''


The entry 4dfi is ON HOLD
==Crystal structure of cell adhesion molecule nectin-2/CD112 mutant FAMP==
<StructureSection load='4dfi' size='340' side='right'caption='[[4dfi]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4dfi]] 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=4DFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DFI 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]] 1.8&#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=4dfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dfi OCA], [https://pdbe.org/4dfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dfi RCSB], [https://www.ebi.ac.uk/pdbsum/4dfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dfi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NECT2_HUMAN NECT2_HUMAN] Modulator of T-cell signaling. Can be either a costimulator of T-cell function, or a coinhibitor, depending on the receptor it binds to. Upon binding to CD226, stimulates T-cell proliferation and cytokine production, including that of IL2, IL5, IL10, IL13, and IFNG. Upon interaction with PVRIG, inhibits T-cell proliferation. These interactions are competitive (PubMed:26755705). Probable cell adhesion protein (PubMed:9657005).<ref>PMID:26755705</ref> <ref>PMID:9657005</ref>  (Microbial infection) Acts as a receptor for herpes simplex virus 1 (HHV-1) mutant Rid1, herpes simplex virus 1 (HHV-2) and pseudorabies virus (PRV).<ref>PMID:11602758</ref> <ref>PMID:9657005</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The nectin and nectin-like molecule (Necl) family includes important cell adhesion molecules (CAMs) characterized by their Ig-like nature. Such CAMs regulate a broad spectrum of cell-cell interactions, including the interaction between NK cells and cytotoxic T lymphocytes (CTLs) and their target cells. CAM members nectin-2 (CD112) and Necl-5 (CD155) are believed to form homodimers (for nectin-2) or heterodimers in their functions for cell adhesion, as well as to interact with immune costimulatory receptor DNAX accessory molecule 1 (DNAM-1) (CD226) to regulate functions of both NK and CTL cells. However, the structural basis of the interactive mode of DNAM-1 with nectin-2 or Necl-5 is not yet understood. In this study, a soluble nectin-2 Ig-like V-set domain (nectin-2v) was successfully prepared and demonstrated to bind to both soluble ectodomain and cell surface-expressed full-length DNAM-1. The 1.85-A crystal structure of nectin-2v displays a perpendicular homodimer arrangement, revealing the homodimer characteristics of the nectin and Necls. Further mutational analysis indicated that disruption of the homodimeric interface of nectin-2v led to a failure of the homodimer formation, as confirmed by crystal structure and biochemical properties of the mutant protein of nectin-2v. Interestingly, the monomer mutant also loses DNAM-1 binding, as evidenced by cell staining with tetramers and surface plasmon resonance assays. The data indicate that interaction with DNAM-1 requires either the homodimerization or engagement of the homodimeric interface of nectin-2v. These results have implications for immune intervention of tumors or autoimmune diseases in the DNAM-1/nectin-2-dependent pathway.


Authors: Liu, J., Qian, X., Chen, Z., Xu, X., Gao, F., Zhang, S., Zhang, R., Qi, J., Gao, G.F., Yan, J.
Crystal Structure of Cell Adhesion Molecule Nectin-2/CD112 and Its Binding to Immune Receptor DNAM-1/CD226.,Liu J, Qian X, Chen Z, Xu X, Gao F, Zhang S, Zhang R, Qi J, Gao GF, Yan J J Immunol. 2012 Jun 1;188(11):5511-20. Epub 2012 Apr 30. PMID:22547693<ref>PMID:22547693</ref>


Description: Crystal structure of cell adhesion molecule nectin-2/CD112 mutant FAMP
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4dfi" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Poliovirus receptor-related protein|Poliovirus receptor-related protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chen Z]]
[[Category: Gao F]]
[[Category: Gao GF]]
[[Category: Liu J]]
[[Category: Qi J]]
[[Category: Qian X]]
[[Category: Xu X]]
[[Category: Yan J]]
[[Category: Zhang R]]
[[Category: Zhang S]]
Retrieved from "https://proteopedia.org/4dfi"