4mnh: Difference between revisions
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== | ==Structure of the DP10.7 TCR== | ||
[[4mnh]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MNH OCA]. | <StructureSection load='4mnh' size='340' side='right'caption='[[4mnh]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4mnh]] is a 4 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=4MNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MNH 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]] 3.3Å</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=4mnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mnh OCA], [https://pdbe.org/4mnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mnh RCSB], [https://www.ebi.ac.uk/pdbsum/4mnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mnh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6PJ56_HUMAN Q6PJ56_HUMAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The nature of the antigens recognized by gammadelta T cells and their potential recognition of major histocompatibility complex (MHC)-like molecules has remained unclear. Members of the CD1 family of lipid-presenting molecules are suggested ligands for Vdelta1 TCR-expressing gammadelta T cells, the major gammadelta lymphocyte population in epithelial tissues. We crystallized a Vdelta1 TCR in complex with CD1d and the self-lipid sulfatide, revealing the unusual recognition of CD1d by germline Vdelta1 residues spanning all complementarity-determining region (CDR) loops, as well as sulfatide recognition separately encoded by nongermline CDR3delta residues. Binding and functional analysis showed that CD1d presenting self-lipids, including sulfatide, was widely recognized by gut Vdelta1+ gammadelta T cells. These findings provide structural demonstration of MHC-like recognition of a self-lipid by gammadelta T cells and reveal the prevalence of lipid recognition by innate-like T cell populations. | |||
Crystal Structure of Vdelta1 T Cell Receptor in Complex with CD1d-Sulfatide Shows MHC-like Recognition of a Self-Lipid by Human gammadelta T Cells.,Luoma AM, Castro CD, Mayassi T, Bembinster LA, Bai L, Picard D, Anderson B, Scharf L, Kung JE, Sibener LV, Savage PB, Jabri B, Bendelac A, Adams EJ Immunity. 2013 Dec 12;39(6):1032-42. doi: 10.1016/j.immuni.2013.11.001. Epub 2013, Nov 14. PMID:24239091<ref>PMID:24239091</ref> | |||
<ref | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[ | <div class="pdbe-citations 4mnh" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Adams EJ]] | ||
[[Category: | [[Category: Luoma AM]] | ||
[[Category: | |||
Latest revision as of 14:09, 6 November 2024
Structure of the DP10.7 TCRStructure of the DP10.7 TCR
Structural highlights
FunctionPublication Abstract from PubMedThe nature of the antigens recognized by gammadelta T cells and their potential recognition of major histocompatibility complex (MHC)-like molecules has remained unclear. Members of the CD1 family of lipid-presenting molecules are suggested ligands for Vdelta1 TCR-expressing gammadelta T cells, the major gammadelta lymphocyte population in epithelial tissues. We crystallized a Vdelta1 TCR in complex with CD1d and the self-lipid sulfatide, revealing the unusual recognition of CD1d by germline Vdelta1 residues spanning all complementarity-determining region (CDR) loops, as well as sulfatide recognition separately encoded by nongermline CDR3delta residues. Binding and functional analysis showed that CD1d presenting self-lipids, including sulfatide, was widely recognized by gut Vdelta1+ gammadelta T cells. These findings provide structural demonstration of MHC-like recognition of a self-lipid by gammadelta T cells and reveal the prevalence of lipid recognition by innate-like T cell populations. Crystal Structure of Vdelta1 T Cell Receptor in Complex with CD1d-Sulfatide Shows MHC-like Recognition of a Self-Lipid by Human gammadelta T Cells.,Luoma AM, Castro CD, Mayassi T, Bembinster LA, Bai L, Picard D, Anderson B, Scharf L, Kung JE, Sibener LV, Savage PB, Jabri B, Bendelac A, Adams EJ Immunity. 2013 Dec 12;39(6):1032-42. doi: 10.1016/j.immuni.2013.11.001. Epub 2013, Nov 14. PMID:24239091[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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