TY - JOUR
T1 - Crystal structure of I-A(k) in complex with a dominant epitope of lysozyme
AU - Fremont, Daved H.
AU - Monnaie, Didier
AU - Nelson, Christopher A.
AU - Hendrickson, Wayne A.
AU - Unanue, Emil R.
N1 - Funding Information:
The authors thank Shirley J. Petzold for expertise in protein purification; Chris Lima for aid in synchrotron data collection; Paul Allen and Larry Shapiro for critical reading of the manuscript; and John Kappler and Kyunghee Choi for encouragement and support. D. H. F. is the recipient of a Burroughs-Wellcome Fund Career Award in the Biomedical Sciences.
PY - 1998/3
Y1 - 1998/3
N2 - We have determined the structure of murine MHC class II I-A(k) in complex with a naturally processed peptide from hen egg lysozyme (HEL residues 50-62) at 1.9 Å resolution. These results provide a structural basis for the I-A(k) peptide-binding motif. Binding is established by the deep burial of five anchor side chains into specific pockets of the I-A(k) binding groove, with a zen-like fit of an aspartic acid in the P1 pocket. We also show that in the I-A(k) a chain, a bulge occurs in the first strand of the peptide-binding platform, an insertion probably common to all I-A and HLA-DQ alleles. The I-A(k) β chain has a deletion in the helical region adjacent to the P7 pocket and an insertion in the helical region neighboring the P1 pocket. As a result of these structural features, the extended HEL peptide dips low into the center of the I-A(k) groove and reaches toward solvent at its C-terminal end.
AB - We have determined the structure of murine MHC class II I-A(k) in complex with a naturally processed peptide from hen egg lysozyme (HEL residues 50-62) at 1.9 Å resolution. These results provide a structural basis for the I-A(k) peptide-binding motif. Binding is established by the deep burial of five anchor side chains into specific pockets of the I-A(k) binding groove, with a zen-like fit of an aspartic acid in the P1 pocket. We also show that in the I-A(k) a chain, a bulge occurs in the first strand of the peptide-binding platform, an insertion probably common to all I-A and HLA-DQ alleles. The I-A(k) β chain has a deletion in the helical region adjacent to the P7 pocket and an insertion in the helical region neighboring the P1 pocket. As a result of these structural features, the extended HEL peptide dips low into the center of the I-A(k) groove and reaches toward solvent at its C-terminal end.
UR - http://www.scopus.com/inward/record.url?scp=0032033445&partnerID=8YFLogxK
U2 - 10.1016/S1074-7613(00)80536-1
DO - 10.1016/S1074-7613(00)80536-1
M3 - Article
C2 - 9529148
AN - SCOPUS:0032033445
SN - 1074-7613
VL - 8
SP - 305
EP - 317
JO - Immunity
JF - Immunity
IS - 3
ER -