期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 277, 期 2, 页码 1433-1442出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110316200
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资金
- NIAID NIH HHS [AI47900] Funding Source: Medline
- NIGMS NIH HHS [GM52801] Funding Source: Medline
Ly49A, an inhibitory C-type lectin-like mouse natural killer cell receptor, functions through interaction with the major histocompatibility complex class I molecule, H-2D(d). The x-ray crystal structure of the Ly49A(.)H-2D(d) complex revealed that homodimeric Ly49A interacts at two distinct sites of H-2Dd: Site 1, spanning one side of the alpha1 and alpha2 helices, and Site 2, involving the alpha1, alpha2, alpha3, and beta(2)m domains. Mutants of Ly49A, H-2D(d), and beta(2)-microglobulin at intermolecular contacts and the Ly49A dimer interface were examined for binding affinity and kinetics. Although mutations at Site 1 had little affect, several at Site 2 and at the dimer interface hampered the Ly49A(.)H-2D(d) interaction, with no effect on gross structure or T cell receptor interaction. The region surrounding the most critical residues (in H-2D(d), Asp(122); in Ly49A, Asp(229), Ser(236), Thr(238), Arg(231), and Asp(241); and in beta(2)-microglobulin, Gln(29) and Lys(58)) of the Ly49A(.)H-2D(d) interface at Site 2 includes a network of water molecules, suggesting a molecular basis for allelic specificity in natural killer cell recognition.
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