6tro: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='6tro' size='340' side='right'caption='[[6tro]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='6tro' size='340' side='right'caption='[[6tro]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6tro]] is a 5 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=6TRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TRO FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TRO 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&#8491;</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]] 3&#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=6tro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tro OCA], [https://pdbe.org/6tro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tro RCSB], [https://www.ebi.ac.uk/pdbsum/6tro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tro ProSAT]</span></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=6tro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tro OCA], [https://pdbe.org/6tro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tro RCSB], [https://www.ebi.ac.uk/pdbsum/6tro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tro ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q53Z42_HUMAN Q53Z42_HUMAN] Involved in the presentation of foreign antigens to the immune system (By similarity).[SAAS:SAAS003006_004_004364]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
T cell-mediated immunity is governed primarily by T cell receptor (TCR) recognition of peptide human leukocyte antigen complexes (pHLA) and is essential for immunosurveillance and disease control. This interaction is generally stabilised by interactions between the HLA surface and TCR germline encoded complementarity determining region (CDR) loops 1 and 2, whereas peptide selectivity is guided by direct interactions with the TCR CDR3 loops. Here, we solved the structure of a newly identified TCR in complex with a clinically relevant peptide derived from the cancer testis antigen melanoma antiGEn-A4 (MAGE-A4). The TCR bound pHLA in a position shifted toward the peptide's N-terminus. This enabled the TCR to achieve peptide selectivity via an indirect mechanism, whereby the TCR sensed the first residue of the peptide through HLA residue Trp167, which acted as a tuneable gateway. Amino acid substitutions at peptide position 1 predicted to alter the HLA Trp167 sidechain conformation abrogated TCR binding, indicating that this indirect binding mechanism is essential for peptide recognition. These findings extend our understanding of the molecular rules that underpin antigen recognition by TCRs and have important implications for the development of TCR-based therapies.
T Cell Receptor interactions with Human Leukocyte Antigen govern indirect peptide selectivity for the cancer testis antigen MAGE-A4.,Coles CH, McMurran C, Lloyd A, Hock M, Hibbert L, Raman MCC, Hayes C, Lupardus P, Cole DK, Harper S J Biol Chem. 2020 Jun 12. pii: RA120.014016. doi: 10.1074/jbc.RA120.014016. PMID:32532817<ref>PMID:32532817</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6tro" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
Line 24: Line 13:
*[[MHC I 3D structures|MHC I 3D structures]]
*[[MHC I 3D structures|MHC I 3D structures]]
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cole DK]]
[[Category: Cole DK]]

Latest revision as of 13:30, 23 October 2024

Crystal structure of the T-cell receptor GVY01 bound to HLA A2*01-GVYDGREHTVCrystal structure of the T-cell receptor GVY01 bound to HLA A2*01-GVYDGREHTV

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

6tro, resolution 3.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=6tro&oldid=4225692"