1AGF

ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGKKRYKL-5R MUTATION)

1AGF の概要

• エントリーDOI: 10.2210/pdb1agf/pdb
• 分子名称: B*0801, BETA-2 MICROGLOBULIN, HIV-1 GAG PEPTIDE (GGKKRYKL - 5R MUTATION), ... (4 entities in total)
• 機能のキーワード: hla b8, hiv, mhc class i, histocompatibility complex
• 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: P30460; Secreted: P61769
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44629.32

構造登録者

Reid, S.W.,Mcadam, S.,Smith, K.J.,Klenerman, P.,O'Callaghan, C.A.,Harlos, K.,Jakobsen, B.K.,Mcmichael, A.J.,Bell, J.,Stuart, D.I.,Jones, E.Y. (登録日: 1997-03-24, 公開日: 1997-06-16, 最終更新日: 2024-11-20)

主引用文献

Reid, S.W.,McAdam, S.,Smith, K.J.,Klenerman, P.,O'Callaghan, C.A.,Harlos, K.,Jakobsen, B.K.,McMichael, A.J.,Bell, J.I.,Stuart, D.I.,Jones, E.Y.
Antagonist HIV-1 Gag peptides induce structural changes in HLA B8.
J.Exp.Med., 184:2279-2286, 1996

PubMed Abstract: In the cellular immune response, recognition by CTL-TCRs of viral antigens presented as peptides by HLA class I molecules, triggers destruction of the virally infected cell (Townsend, A.R.M., J. Rothbard, F.M. Gotch, G. Bahadur, D. Wraith, and A.J. McMichael. 1986. Cell. 44:959-968). Altered peptide ligands (APLs) which antagonise CTL recognition of infected cells have been reported (Jameson, S.C., F.R. Carbone, and M.J. Bevan. 1993. J. Exp. Med. 177:1541-1550). In one example, lysis of antigen presenting cells by CTLs in response to recognition of an HLA B8-restricted HIV-1 P17 (aa 24-31) epitope can be inhibited by naturally occurring variants of this peptide, which act as TCR antagonists (Klenerman, P., S. Rowland Jones, S. McAdam, J. Edwards, S. Daenke, D. Lalloo, B. Koppe, W. Rosenberg, D. Boyd, A. Edwards, P. Giangrande, R.E. Phillips, and A. McMichael. 1994. Nature (Lond.). 369:403-407). We have characterised two CTL clones and a CTL line whose interactions with these variants of P17 (aa 24-31) exhibit a variety of responses. We have examined the high resolution crystal structures of four of these APLs in complex with HLA B8 to determine alterations in the shape, chemistry, and local flexibility of the TCR binding surface. The variant peptides cause changes in the recognition surface by three mechanisms: changes contributed directly by the peptide, effects transmitted to the exposed peptide surface, and induced effects on the exposed framework of the peptide binding groove. While the first two mechanisms frequently lead to antagonism, the third has more profound effects on TCR recognition.

PubMed: 8976183
DOI: 10.1084/jem.184.6.2279

実験手法

X-RAY DIFFRACTION (2.2 Å)