The crystal structure of H-2Dd MHC class I complexed with the HIV-1-derived peptide P18-I10 at 2.4 A resolution: implications for T cell and NK cell recognition.

Abstract:

:The structure of H-2Dd complexed with the HIV-derived peptide P18-I10 (RGPGRAFVTI) has been determined by X-ray crystallography at 2.4 A resolution. This MHC class I molecule has an unusual binding motif with four anchor residues in the peptide (G2, P3, R/K/H5, and I/L/F9 or 10). The cleft architecture of H-2Dd includes a deep narrow passage accomodating the N-terminal part of the peptide, explaining the obligatory G2P3 anchor motif. Toward the C-terminal half of the peptide, p5R to p8V form a type I' reverse turn; residues p6A to p9T, and in particular p7F, are readily exposed. The structure is discussed in relation to functional data available for T cell and natural killer cell recognition of the H-2Dd molecule.

journal_name

Immunity

journal_title

Immunity

authors

Achour A,Persson K,Harris RA,Sundbäck J,Sentman CL,Lindqvist Y,Schneider G,Kärre K

doi

10.1016/s1074-7613(00)80602-0

subject

Has Abstract

pub_date

1998-08-01 00:00:00

pages

199-208

issue

2

eissn

1074-7613

issn

1097-4180

pii

S1074-7613(00)80602-0

journal_volume

9

pub_type

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