Crystallization and preliminary X-ray crystallographic studies of HLA-A*1101 complexed with an HIV-1 decapeptide.
A major goal of vaccine research for the prevention of AIDS is to determine the immune correlates of protection against HIV-1 infection. In this context, it is of interest to understand how HLA-A*1101, a significantly more prevalent class I allele in a cohort of highly HIV-1-exposed persistently seronegative individuals, functions in relation to protective immunity to HIV-1. Towards this goal, a soluble recombinant HLA-A*1101 molecule has been expressed and used to assemble a complex with beta2-microglobulin and a Nef decapeptide. The HLA-A*1101/beta2m/Nef complex was crystallized by the hanging-drop vapor-diffusion method. The crystal formed in the monoclinic space group P2(1), with unit-cell parameters a = 77.2, b = 88.5, c = 64.8 A, beta = 90.1 degrees, and contains two molecules in the asymmetric unit. A data set to 2.2 A resolution was collected and structure determination by molecular replacement is currently in progress. Understanding the three-dimensional structure of the HLA-A*1101/beta2m/Nef complex may provide insight into the functional role of this class I allele in relation to protective immunity to HIV-1.
Li
Lenong
L
School of Pharmacy, University of Connecticut, 372 Fairfield Road, U-92, Storrs 06269, USA.
Promadej
Nattawan
N
McNicholl
Janet M
JM
Bouvier
Marlene
M
D000483:Alleles; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D018360:Crystallography, X-Ray / Q000379:methods*; D018076:DNA, Complementary / Q000378:metabolism; D015497:HIV-1 / Q000737:chemistry*; D015234:HLA-A Antigens / Q000737:chemistry*; D006801:Humans; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000737:chemistry; D013997:Time Factors
D018076:DNA, Complementary; D015234:HLA-A Antigens; D010455:Peptides; D011994:Recombinant Proteins