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T-cell recognition of the antigenic peptides presented by MHC class I molecules normally triggers protective immune responses, but can result in immune enhancement of disease. Cross-reactive T-cell responses may underlie immunopathology in dengue haemorrhagic fever. To analyze these effects at the molecular level, the functional MHC class I molecule HLA-A*1101 was crystallized bound to six naturally occurring peptide variants from the dengue virus NS3 protein. The crystals contained high levels of solvent and required optimization of the cryoprotectant and dehydration protocols for each complex to yield well ordered diffraction, a process that was facilitated by the use of a free-mounting system.

Original publication

DOI

10.1107/S1744309107013693

Type

Journal article

Journal

Acta Crystallogr Sect F Struct Biol Cryst Commun

Publication Date

01/05/2007

Volume

63

Pages

386 - 392

Keywords

Amino Acid Sequence, Chromatography, Gel, Crystallization, Crystallography, X-Ray, Dengue Virus, HLA-A Antigens, Humidity, Peptides, Protein Conformation, Viral Proteins