2BVQ

Structures of Three HIV-1 HLA-B5703-Peptide Complexes and Identification of Related HLAs Potentially Associated with Long-Term Non-Progression

Summary for 2BVQ

• Entry DOI: 10.2210/pdb2bvq/pdb
• Related: 1A1M 1A1N 1A1O 1A6Z 1A9B 1A9E 1AGB 1AGC 1AGD 1AGE 1AGF 1AKJ 1AO7 1B0G 1B0R 1BD2 1C16 1CE6 1CG9 1DE4 1DUY 1DUZ 1E27 1E28 1EEY 1EEZ 1EFX 1EXU 1GZP 1GZQ 1HHG 1HHH 1HHI 1HHJ 1HHK 1HLA 1HSA 1HSB 1I1F 1I1Y 1I4F 1I7R 1I7T 1I7U 1IM3 1IM9 1JF1 1JGD 1JGE 1JHT 1JNJ 1K5N 1KPR 1KTL 1LDS 1LP9 1M05 1M6O 1MHE 1MI5 1N2R 1OF2 1OGA 1OGT 1ONQ 1P7Q 1PY4 1Q94 1QEW 1QLF 1QQD 1QR1 1QRN 1QSE 1QSF 1QVO 1R3H 1S9W 1S9X 1S9Y 1SYS 1SYV 1TMC 1TVB 1TVH 1UQS 1UR7 1UXS 1UXW 1W0V 1W0W 1W72 1X7Q 1XH3 1XR8 1XR9 1XZ0 1YDP 1YPZ 1ZS8 1ZSD 1ZT4 2BNQ 2BNR 2BSR 2BSS 2BST 2BSU 2BSV 2BVO 2BVP 2CLR 2HLA 3HLA
• Descriptor: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, B-57 ALPHA CHAIN, BETA-2-MICROGLOBULIN, HIV-P24, ... (4 entities in total)
• Functional Keywords: glycoprotein/peptide, mhc, hla-b57, ltnp hiv-1, glycoprotein-peptide complex, mhc i, polymorphism, transmembrane, immunoglobulin domain, pyrrolidone carboxylic acid, immune response
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 3
• Total formula weight: 44957.17

Authors

Stewart-Jones, G.B.,Gillespie, G.,Overton, I.M.,Kaul, R.,Roche, P.,Mcmichael, A.J.,Rowland-Jones, S.,Jones, E.Y. (deposition date: 2005-07-01, release date: 2005-09-07, Last modification date: 2024-11-13)

Primary citation

Stewart-Jones, G.B.,Gillespie, G.,Overton, I.M.,Kaul, R.,Roche, P.,McMichael, A.J.,Rowland-Jones, S.,Jones, E.Y.
Structures of three HIV-1 HLA-B*5703-peptide complexes and identification of related HLAs potentially associated with long-term nonprogression.
J Immunol., 175:2459-2468, 2005

PubMed Abstract: Long-term nonprogression during acute HIV infection has been strongly associated with HLA-B*5701 or HLA-B*5703. In this study, we present the high resolution crystal structures of HLA-B*5703 complexes with three HIV-1 epitopes: ISPRTLNAW (ISP), KAFSPEVIPMF (KAF-11), and KAFSPEVI (KAF-8). These reveal peptide anchoring at position 2 and their C termini. The different peptide lengths and primary sequences are accommodated by variation in the specific contacts made to the HLA-B*5703, flexibility in water structure, and conformational adjustment of side chains within the peptide-binding groove. The peptides adopt markedly different conformations, and trap variable numbers of water molecules, near a cluster of tyrosine side chains located in the central region of the peptide-binding groove. The KAF-11 epitope completely encompasses the shorter KAF-8 epitope but the peptides are presented in different conformations; the KAF-11 peptide arches out of the peptide-binding groove, exposing a significant main chain surface area. Bioinformatic analysis of the MHC side chains observed to contribute to the peptide anchor specificity, and other specific peptide contacts, reveals HLA alleles associated with long-term nonprogression and a number of related HLA alleles that may share overlapping peptide repertoires with HLA-B*5703 and thus may display a similar capacity for efficient immune control of HIV-1 infection.

PubMed: 16081817
DOI: 10.4049/jimmunol.175.4.2459

Experimental method

X-RAY DIFFRACTION (2 Å)