1ZVS

Crystal structure of the first class MHC mamu and Tat-Tl8 complex

1ZVS の概要

• エントリーDOI: 10.2210/pdb1zvs/pdb
• 分子名称: MHC class I antigen, Beta-2-microglobulin, Tat-Tl8, ... (4 entities in total)
• 機能のキーワード: the first class mhc, mamu, tat-tl8, immune system
• 由来する生物種: Macaca mulatta (rhesus monkey); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 89431.03

構造登録者

Lou, Z.,Chu, F.,Gao, G.F.,Rao, Z. (登録日: 2005-06-02, 公開日: 2006-06-13, 最終更新日: 2024-11-20)

主引用文献

Chu, F.,Lou, Z.,Chen, Y.W.,Liu, Y.,Gao, B.,Zong, L.,Khan, A.H.,Bell, J.I.,Rao, Z.,Gao, G.F.
First glimpse of the peptide presentation by rhesus macaque MHC class I: crystal structures of Mamu-A*01 complexed with two immunogenic SIV epitopes and insights into CTL escape.
J Immunol., 178:944-952, 2007

PubMed Abstract: The infection of rhesus macaques (Macaca mulatta) by the SIV is the best animal model for studying HIV infection and for AIDS vaccine development. A prevalent MHC class I allele, Mamu-A*01, is known to correlate with containment of SIV, which has been extensively explored in studies of CTL-based vaccination concepts. We determined the crystal structures of Mamu-A*01 complexed with two immunodominant SIV epitopes: the nonamer CM9 of group-specific Ag (Gag, 181-189; CTPYDINQM) and the octamer TL8 of transcription activator (Tat, 28-35; TTPESANL). The overall structures of the two Mamu-A*01 complexes are similar to other MHC class I molecules. Both structures confirm the presence of an absolutely conserved proline anchor residue in the P3 position of the Ag, bound to a D pocket of the Mamu-A*01 H chain with optimal surface complementarity. Like other MHC/peptide complex structures, the P2 and C-terminal residues of the epitopes are also important for anchoring to the MHC molecule, whereas the middle residues form an arch and their side chains are directed into solvent. These two structures reveal details of how Mamu-A*01 interacts with two well-studied epitopes at the atomic level. We discuss the structural basis of CTL escape, based on molecular models made possible by these two structures. The results we present in this study are most relevant for the rational design of Mamu-A*01-restricted CTL epitopes with improved binding, as a step toward development of AIDS vaccines.

PubMed: 17202356
DOI: 10.4049/jimmunol.178.2.944

実験手法

X-RAY DIFFRACTION (2.8 Å)