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2BCK

Crystal Structure of HLA-A*2402 Complexed with a telomerase peptide

2BCK の概要
エントリーDOI10.2210/pdb2bck/pdb
分子名称HLA class I histocompatibility antigen, A-24 alpha chain, Beta-2-microglobulin, Telomerase reverse transcriptase, ... (6 entities in total)
機能のキーワードimmunoglobulin domains, beta barrels, mhc fold, 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: P05534
Secreted: P61769
Nucleus, nucleolus: O14746
タンパク質・核酸の鎖数6
化学式量合計94392.49
構造登録者
Rizkallah, P.J.,Jakobsen, B.K.,Cole, D.K.,Gao, G.F. (登録日: 2005-10-19, 公開日: 2006-01-10, 最終更新日: 2024-10-23)
主引用文献Cole, D.K.,Rizkallah, P.J.,Gao, F.,Watson, N.I.,Boulter, J.M.,Bell, J.I.,Sami, M.,Gao, G.F.,Jakobsen, B.K.
Crystal structure of HLA-A*2402 complexed with a telomerase peptide.
Eur.J.Immunol., 36:170-179, 2006
Cited by
PubMed Abstract: HLA-A*2402 is the most commonly expressed HLA allele in oriental populations. It is also widely expressed in the Caucasian population, making it one of, if not the most abundant HLA I types. In order to study its structure in terms of overall fold and peptide presentation, a soluble form of this HLA I (alpha1, alpha2, alpha3 and beta(2)m domains) has been expressed, refolded and crystallized in complex with a cancer-related telomerase peptide (VYGFVRACL), and its structure has been solved to 2.8 A resolution. The overall structure of HLA-A*2402 is virtually identical to other reported peptide-HLA I structures. However, there are distinct features observable from this structure at the HLA I peptide binding pockets. The size and depth of pocket B makes it highly suitable for binding to large aromatic side chains, which explains the high prevalence of tyrosine at peptide position 2. Also, for HLA binding at peptide position 5, there is an additional anchor point, which allows the proximal amino acids to protrude out, providing a prominent feature for TCR interaction. Finally, pocket F allows the anchor residue at position 9 to be bound unusually deeply within the HLA structure.
PubMed: 16323248
DOI: 10.1002/eji.200535424
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.8 Å)
構造検証レポート
Validation report summary of 2bck
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-08に公開中

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