2AK4

Crystal Structure of SB27 TCR in complex with HLA-B*3508-13mer peptide

Summary for 2AK4

• Entry DOI: 10.2210/pdb2ak4/pdb
• Related: 1ZHL
• Descriptor: HLA-B35 variant, Beta-2-microglobulin, EBV peptide LPEPLPQGQLTAY, ... (7 entities in total)
• Functional Keywords: t cell receptor, bulged epitopes, pmhc-tcr complex, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P61769
• Total number of polymer chains: 20
• Total formula weight: 390028.74

Authors

Tynan, F.E.,Burrows, S.R.,Buckle, A.M.,Clements, C.S.,Borg, N.A.,Miles, J.J.,Beddoe, T.,Whisstock, J.C.,Wilce, M.C.,Silins, S.L.,Burrows, J.M.,Kjer-Nielsen, L.,Konstenko, L.,Purcell, A.W.,McCluskey, J.,Rossjohn, J. (deposition date: 2005-08-03, release date: 2005-10-11, Last modification date: 2024-10-23)

Primary citation

Tynan, F.E.,Burrows, S.R.,Buckle, A.M.,Clements, C.S.,Borg, N.A.,Miles, J.J.,Beddoe, T.,Whisstock, J.C.,Wilce, M.C.,Silins, S.L.,Burrows, J.M.,Kjer-Nielsen, L.,Kostenko, L.,Purcell, A.W.,McCluskey, J.,Rossjohn, J.
T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide
Nat.Immunol., 6:1114-1122, 2005

PubMed Abstract: Unusually long major histocompatibility complex (MHC) class I-restricted epitopes are important in immunity, but their 'bulged' conformation represents a potential obstacle to alphabeta T cell receptor (TCR)-MHC class I docking. To elucidate how such recognition is achieved while still preserving MHC restriction, we have determined here the structure of a TCR in complex with HLA-B(*)3508 presenting a peptide 13 amino acids in length. This complex was atypical of TCR-peptide-MHC class I interactions, being dominated at the interface by peptide-mediated interactions. The TCR assumed two distinct orientations, swiveling on top of the centrally bulged, rigid peptide such that only limited contacts were made with MHC class I. Although the TCR-peptide recognition resembled an antibody-antigen interaction, the TCR-MHC class I contacts defined a minimal 'generic footprint' of MHC-restriction. Thus our findings simultaneously demonstrate the considerable adaptability of the TCR and the 'shape' of MHC restriction.

PubMed: 16186824
DOI: 10.1038/ni1257

Experimental method

X-RAY DIFFRACTION (2.5 Å)