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3GSR

Crystal structure of the binary complex between HLA-A2 and HCMV NLV-M5V peptide variant

Summary for 3GSR
Entry DOI10.2210/pdb3gsr/pdb
Related3GSN 3GSO 3GSQ 3GSU 3GSV 3GSW 3GSX
DescriptorHLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, HCMV pp65 fragment 495-503, variant M5V (NLVPVVATV), ... (4 entities in total)
Functional Keywordshla, human cytomegalovirus, pp65, t cell receptor (tcr), immune response, public response, immunodominance, restrained response, host-virus interaction, membrane, mhc i, polymorphism, immunoglobulin domain, immune system
Biological sourceHomo sapiens (human)
More
Cellular locationMembrane; Single-pass type I membrane protein: P01892
Secreted: P61769
Total number of polymer chains3
Total formula weight44543.59
Authors
Primary citationGras, S.,Saulquin, X.,Reiser, J.B.,Debeaupuis, E.,Echasserieau, K.,Kissenpfennig, A.,Legoux, F.,Chouquet, A.,Le Gorrec, M.,Machillot, P.,Neveu, B.,Thielens, N.,Malissen, B.,Bonneville, M.,Housset, D.
Structural bases for the affinity-driven selection of a public TCR against a dominant human cytomegalovirus epitope.
J.Immunol., 183:430-437, 2009
Cited by
PubMed Abstract: Protective T cell responses elicited along chronic human CMV (HCMV) infections are sometimes dominated by CD8 T cell clones bearing highly related or identical public TCR in unrelated individuals. To understand the principles that guide emergence of these public T cell responses, we have performed structural, biophysical, and functional analyses of an immunodominant public TCR (RA14) directed against a major HLA-A*0201-restricted HCMV Ag (pp65(495-503)) and selected in vivo from a diverse repertoire after chronic stimulations. Unlike the two immunodominant public TCRs crystallized so far, which focused on one peptide hotspot, the HCMV-specific RA14 TCR interacts with the full array of available peptide residues. The conservation of some peptide-MHC complex-contacting amino acids by lower-affinity TCRs suggests a shared TCR-peptide-MHC complex docking mode and supports an Ag-driven selection of optimal TCRs. Therefore, the emergence of a public TCR of an oligoclonal Ag-specific response after repeated viral stimulations is based on a receptor displaying a high structural complementarity with the entire peptide and focusing on three peptide hotspots. This highlights key parameters underlying the selection of a protective T cell response against HCMV infection, which remains a major health issue in patients undergoing bone marrow transplantation.
PubMed: 19542454
DOI: 10.4049/jimmunol.0900556
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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数据于2024-10-30公开中

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