3omz

<table><tr><td colspan='2'>[[3omz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OMZ FirstGlance]. <br>

</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=3omz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3omz OCA], [https://pdbe.org/3omz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3omz RCSB], [https://www.ebi.ac.uk/pdbsum/3omz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3omz ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

gammadelta T cells play important roles in bridging innate and adaptive immunity, but their recognition mechanisms remain poorly understood. Human gammadelta T cells of the V(delta)1 subset predominate in intestinal epithelia and respond to MICA and MICB (MHC class I chain-related, A and B; MIC) self-antigens, mediating responses to tumorigenesis or viral infection. The crystal structure of an MIC-reactive V(delta)1 gammadelta T-cell receptor (TCR) showed expected overall structural homology to antibodies, alphabeta, and other gammadelta TCRs, but complementary determining region conformations and conservation of V(delta)1 use revealed an uncharacteristically flat potential binding surface. MIC, likewise, serves as a ligand for the activating immunoreceptor natural killer group 2, D (NKG2D), also expressed on gammadelta T cells. Although MIC recognition drives both the TCR-dependent stimulatory and NKG2D-dependent costimulatory signals necessary for activation, interaction analyses showed that MIC binding by the two receptors was mutually exclusive. Analysis of relative binding kinetics suggested sequential recognition, defining constraints for the temporal organization of gammadelta T-cell/target cell interfaces.

Crystal structure of a {gamma}{delta} T-cell receptor specific for the human MHC class I homolog MICA.,Xu B, Pizarro JC, Holmes MA, McBeth C, Groh V, Spies T, Strong RK Proc Natl Acad Sci U S A. 2011 Feb 8;108(6):2414-9. Epub 2011 Jan 24. PMID:21262824<ref>PMID:21262824</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 3omz" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Holmes, M A]]

[[Category: Strong, R K]]

[[Category: Xu, B]]

[[Category: Mic-a/b binding]]