3RWJ

Rhesus macaque MHC class I molecule Mamu-B*17-HW8

Summary for 3RWJ

• Entry DOI: 10.2210/pdb3rwj/pdb
• Related: 3RWC 3RWD 3RWE 3RWF 3RWG 3RWH 3RWI
• Descriptor: Major histocompatibility complex class I, Beta-2-microglobulin, Vif HW8 peptide from Virion infectivity factor, ... (4 entities in total)
• Functional Keywords: antigenic peptides, t lymphocytes, immune response, immune system
• Biological source: Macaca mulatta (rhesus macaque); More
• Cellular location: Secreted: P61769
• Total number of polymer chains: 3
• Total formula weight: 44936.57

Authors

Wu, Y.,Gao, F.,Liu, J.,Qi, J.X.,Price, D.A.,Gao, G.F. (deposition date: 2011-05-09, release date: 2012-03-21, Last modification date: 2024-10-30)

Primary citation

Wu, Y.,Gao, F.,Liu, J.,Qi, J.X.,Gostick, E.,Price, D.A.,Gao, G.F.
Structural basis of diverse peptide accommodation by the rhesus macaque MHC class I molecule Mamu-B*17: insights into immune protection from simian immunodeficiency virus
J.Immunol., 187:6382-6392, 2011

PubMed Abstract: The MHC class I molecule Mamu-B*17 has been associated with elite control of SIV infection in rhesus macaques, akin to the protective effects described for HLA-B*57 in HIV-infected individuals. In this study, we determined the crystal structures of Mamu-B*17 in complex with eight different peptides corresponding to immunodominant SIV(mac)239-derived CD8(+) T cell epitopes: HW8 (HLEVQGYW), GW10 (GSHLEVQGYW), MW9 (MHPAQTSQW), QW9 (QTSQWDDPW), FW9 (FQWMGYELW), MF8 (MRHVLEPF), IW9 (IRYPKTFGW), and IW11 (IRYPKTFGWLW). The structures reveal that not only P2, but also P1 and P3, can be used as N-terminal anchor residues by Mamu-B*17-restricted peptides. Moreover, the N-terminal anchor residues exhibit a broad chemical specificity, encompassing basic (H and R), bulky polar aliphatic (Q), and small (T) residues. In contrast, Mamu-B*17 exhibits a very narrow preference for aromatic residues (W and F) at the C terminus, similar to that displayed by HLA-B*57. Flexibility within the whole peptide-binding groove contributes to the accommodation of these diverse peptides, which adopt distinct conformations. Furthermore, the unusually large pocket D enables compensation from other peptide residues if P3 is occupied by an amino acid with a small side chain. In addition, residues located at likely TCR contact regions present highly flexible conformations, which may impact TCR repertoire profiles. These findings provide novel insights into the structural basis of diverse peptide accommodation by Mamu-B*17 and highlight unique atomic features that might contribute to the protective effect of this MHC I molecule in SIV-infected rhesus macaques.

PubMed: 22084443
DOI: 10.4049/jimmunol.1101726

Experimental method

X-RAY DIFFRACTION (2.7 Å)