期刊
IMMUNITY
卷 19, 期 6, 页码 803-812出版社
CELL PRESS
DOI: 10.1016/S1074-7613(03)00320-0
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资金
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI048675] Funding Source: NIH RePORTER
- NIAID NIH HHS [AI48675] Funding Source: Medline
The homodimeric immunoreceptor NKG2D drives the activation of effector cells following engagement of diverse, conditionally expressed MHC class I-like protein ligands. NKG2D recognition is highly degenerate in that a single surface on receptor monomers binds pairs of distinct surfaces on each structurally divergent ligand, simultaneously accommodating multiple nonconservative ligand allelic or isoform substitutions. In contrast to TCR-pMHC and other NK receptor-ligand interactions, thermodynamic and kinetic analyses of four NKG2D-ligand pairs (MIC-A*001, MIC-B*005, ULBP1, and RAE-1beta) reported here show that the relative enthalpic and entropic terms, heat capacity, association rates, and activation energy barriers are comparable to typical, rigid protein-protein interactions. Rather than induced-fit binding, NKG2D degeneracy is achieved using distinct interaction mechanisms at each rigid interface.
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