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6EH6

F11 T-Cell Receptor Recognising PKYVKQNTLKLAT Peptide Presented by HLA-DR*0101

Summary for 6EH6
Entry DOI10.2210/pdb6eh6/pdb
DescriptorHuman T Cell Receptor Alpha Chain, Human T Cell Receptor BetaChain, 1,2-ETHANEDIOL, ... (6 entities in total)
Functional Keywordst cell receptor, human leukocyte antigen, influenza epitope, haemagglutinin, 3d structure, immune system
Biological sourceHomo sapiens
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Total number of polymer chains2
Total formula weight50465.18
Authors
Rizkallah, P.J.,Cole, D.K. (deposition date: 2017-09-12, release date: 2018-04-18, Last modification date: 2024-11-20)
Primary citationHolland, C.J.,MacLachlan, B.J.,Bianchi, V.,Hesketh, S.J.,Morgan, R.,Vickery, O.,Bulek, A.M.,Fuller, A.,Godkin, A.,Sewell, A.K.,Rizkallah, P.J.,Wells, S.,Cole, D.K.
In Silicoand Structural Analyses Demonstrate That Intrinsic Protein Motions Guide T Cell Receptor Complementarity Determining Region Loop Flexibility.
Front Immunol, 9:674-674, 2018
Cited by
PubMed Abstract: T-cell immunity is controlled by T cell receptor (TCR) binding to peptide major histocompatibility complexes (pMHCs). The nature of the interaction between these two proteins has been the subject of many investigations because of its central role in immunity against pathogens, cancer, in autoimmunity, and during organ transplant rejection. Crystal structures comparing unbound and pMHC-bound TCRs have revealed flexibility at the interaction interface, particularly from the perspective of the TCR. However, crystal structures represent only a snapshot of protein conformation that could be influenced through biologically irrelevant crystal lattice contacts and other factors. Here, we solved the structures of three unbound TCRs from multiple crystals. Superposition of identical TCR structures from different crystals revealed some conformation differences of up to 5 Å in individual complementarity determining region (CDR) loops that are similar to those that have previously been attributed to antigen engagement. We then used a combination of rigidity analysis and simulations of protein motion to reveal the theoretical potential of TCR CDR loop flexibility in unbound state. These simulations of protein motion support the notion that crystal structures may only offer an artifactual indication of TCR flexibility, influenced by crystallization conditions and crystal packing that is inconsistent with the theoretical potential of intrinsic TCR motions.
PubMed: 29696015
DOI: 10.3389/fimmu.2018.00674
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.78 Å)
Structure validation

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