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1MI5

The crystal structure of LC13 TcR in complex with HLAB8-EBV peptide complex

Summary for 1MI5
Entry DOI10.2210/pdb1mi5/pdb
Related1KGC 1M05
DescriptorMHC heavy chain, beta 2 microglobulin, Epstein Barr Virus peptide, ... (6 entities in total)
Functional Keywordst cell receptor, major histocompatability complex (class i), hla b8, epstein barr virus, immunodominant tcr (lc13), immune system
Biological sourceHomo sapiens (human)
More
Cellular locationMembrane; Single-pass type I membrane protein: P30460
Secreted: P61769
Membrane; Single-pass membrane protein (Potential): P01848 P01850
Total number of polymer chains5
Total formula weight94288.21
Authors
Kjer-Nielsen, L.,Clements, C.S.,Purcell, A.W.,Brooks, A.G.,Whisstock, J.C.,Burrows, S.R.,McCluskey, J.,Rossjohn, J. (deposition date: 2002-08-21, release date: 2003-02-04, Last modification date: 2024-04-03)
Primary citationKjer-Nielsen, L.,Clements, C.S.,Purcell, A.W.,Brooks, A.G.,Whisstock, J.C.,Burrows, S.R.,McCluskey, J.,Rossjohn, J.
A Structural Basis for the Selection of Dominant alphabeta T Cell Receptors in Antiviral Immunity
IMMUNITY, 18:53-64, 2003
Cited by
PubMed Abstract: We have examined the basis for immunodominant or "public" TCR usage in an antiviral CTL response. Residues encoded by each of the highly selected genetic elements of an immunodominant clonotype recognizing Epstein-Barr virus were critical to the antigen specificity of the receptor. Upon recognizing antigen, the immunodominant TCR undergoes extensive conformational changes in the complementarity determining regions (CDRs), including the disruption of the canonical structures of the germline-encoded CDR1alpha and CDR2alpha loops to produce an enhanced fit with the HLA-peptide complex. TCR ligation induces conformational changes in the TCRalpha constant domain thought to form part of the docking site for CD3epsilon. These findings indicate that TCR immunodominance is associated with structural properties conferring receptor specificity and suggest a novel structural link between TCR ligation and intracellular signaling.
PubMed: 12530975
DOI: 10.1016/S1074-7613(02)00513-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

226707

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