3BW9

Crystal Structure of HLA B*3508 in complex with a HCMV 12-mer peptide from the pp65 protein

3BW9 の概要

• エントリーDOI: 10.2210/pdb3bw9/pdb
• 関連するPDBエントリー: 3BWA
• 分子名称: HLA class I histocompatibility antigen, B-35 alpha chain, Beta-2-microglobulin, CPS peptide from 65 kDa lower matrix phosphoprotein, ... (4 entities in total)
• 機能のキーワード: hla b*3508, hcmv, pp65, immunology, glycoprotein, host-virus interaction, immune response, membrane, mhc i, polymorphism, transmembrane, ubl conjugation, disease mutation, glycation, immunoglobulin domain, pyrrolidone carboxylic acid, secreted, phosphoprotein, tegument protein, viral matrix protein, virion, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P30685; Secreted . Note=(Microbial infection) In the presence of M: P61769; Virion tegument : P06725
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 45280.26

構造登録者

Wynn, K.K.,Marland, Z.,Cooper, L.,Silins, S.L.,Gras, S.,Archbold, J.K.,Tynan, F.E.,Miles, J.J.,McCluskey, J.,Burrows, S.R.,Rossjohn, J.,Khanna, R. (登録日: 2008-01-08, 公開日: 2008-04-22, 最終更新日: 2024-10-09)

主引用文献

Wynn, K.K.,Fulton, Z.,Cooper, L.,Silins, S.L.,Gras, S.,Archbold, J.K.,Tynan, F.E.,Miles, J.J.,McCluskey, J.,Burrows, S.R.,Rossjohn, J.,Khanna, R.
Impact of clonal competition for peptide-MHC complexes on the CD8+ T-cell repertoire selection in a persistent viral infection
Blood, 111:4283-4292, 2008

PubMed Abstract: CD8(+) T-cell responses to persistent viral infections are characterized by the accumulation of an oligoclonal T-cell repertoire and a reduction in the naive T-cell pool. However, the precise mechanism for this phenomenon remains elusive. Here we show that human cytomegalovirus (HCMV)-specific CD8(+) T cells recognizing distinct epitopes from the pp65 protein and restricted through an identical HLA class I allele (HLA B*3508) exhibited either a highly conserved public T-cell repertoire or a private, diverse T-cell response, which was uniquely altered in each donor following in vitro antigen exposure. Selection of a public T-cell receptor (TCR) was coincident with an atypical major histocompatibility complex (MHC)-peptide structure, in that the epitope adopted a helical conformation that bulged from the peptide-binding groove, while a diverse TCR profile was observed in response to the epitope that formed a flatter, more "featureless" landscape. Clonotypes with biased TCR usage demonstrated more efficient recognition of virus-infected cells, a greater CD8 dependency, and were more terminally differentiated in their phenotype when compared with the T cells expressing diverse TCR. These findings provide new insights into our understanding on how the biology of antigen presentation in addition to the structural features of the pMHC-I might shape the T-cell repertoire and its phenotype.

PubMed: 18270323
DOI: 10.1182/blood-2007-11-122622

実験手法

X-RAY DIFFRACTION (1.75 Å)