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3KXF

Crystal Structure of SB27 TCR in complex with the 'restriction triad' mutant HLA-B*3508-13mer

Summary for 3KXF
Entry DOI10.2210/pdb3kxf/pdb
Related2AK4 3KWW
DescriptorHLA class I histocompatibility antigen, B-35 alpha chain, Beta-2-microglobulin, SB27 T cell receptor alpha chain, ... (7 entities in total)
Functional Keywordsmhc, hla, tcr, disulfide bond, host-virus interaction, immune response, membrane, mhc i, transmembrane, immunoglobulin domain, immune system
Biological sourceHomo sapiens (human)
More
Cellular locationMembrane; Single-pass type I membrane protein: P30685
Secreted: P61769
Host nucleus: P03206
Total number of polymer chains20
Total formula weight384872.25
Authors
Archbold, J.K.,Tynan, F.E.,Gras, S.,Rossjohn, J. (deposition date: 2009-12-03, release date: 2010-06-09, Last modification date: 2024-10-30)
Primary citationBurrows, S.R.,Chen, Z.,Archbold, J.K.,Tynan, F.E.,Beddoe, T.,Kjer-Nielsen, L.,Miles, J.J.,Khanna, R.,Moss, D.J.,Liu, Y.C.,Gras, S.,Kostenko, L.,Brennan, R.M.,Clements, C.S.,Brooks, A.G.,Purcell, A.W.,McCluskey, J.,Rossjohn, J.
Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability
Proc.Natl.Acad.Sci.USA, 107:10608-10613, 2010
Cited by
PubMed Abstract: alphabeta T cell receptors (TCRs) are genetically restricted to corecognize peptide antigens bound to self-major histocompatibility complex (pMHC) molecules; however, the basis for this MHC specificity remains unclear. Despite the current dogma, evaluation of the TCR-pMHC-I structural database shows that the nongermline-encoded complementarity-determining region (CDR)-3 loops often contact the MHC-I, and the germline-encoded CDR1 and -2 loops frequently participate in peptide-mediated interactions. Nevertheless, different TCRs adopt a roughly conserved docking mode over the pMHC-I, in which three MHC-I residues (65, 69, and 155) are invariably contacted by the TCR in one way or another. Nonetheless, the impact of mutations at these three positions, either individually or together, was not uniformly detrimental to TCR recognition of pHLA-B*0801 or pHLA-B*3508. Moreover, when TCR-pMHC-I recognition was impaired, this could be partially restored by expression of the CD8 coreceptor. The structure of a TCR-pMHC-I complex in which these three (65, 69, and 155) MHC-I positions were all mutated resulted in shifting of the TCR footprint relative to the cognate complex and formation of compensatory interactions. Collectively, our findings reveal the inherent adaptability of the TCR in maintaining peptide recognition while accommodating changes to the central docking site on the pMHC-I.
PubMed: 20483993
DOI: 10.1073/pnas.1004926107
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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