期刊
CELL
卷 112, 期 1, 页码 99-111出版社
CELL PRESS
DOI: 10.1016/S0092-8674(02)01257-6
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资金
- NCI NIH HHS [R01 CA031798, R37 CA031798, CA31798] Funding Source: Medline
- NHLBI NIH HHS [HL48675, P01 HL048675] Funding Source: Medline
The structure of the I domain of integrin alphaLbeta2 bound to the Ig superfamily ligand ICAM-1 reveals the open ligand binding conformation and the first example of an integrin-IgSF interface. The I domain Mg2+ directly coordinates Glu-34 of ICAM-1, and a dramatic swing of I domain residue Glu-241 enables a critical salt bridge. Liganded and unliganded structures for both high- and intermediate-affinity mutant I domains reveal that ligand binding can induce conformational change in the alphaL I domain and that allosteric signals can convert the closed conformation to intermediate or open conformations without ligand binding. Pulling down on the C-terminal alpha7 helix with introduced disulfide bonds ratchets the beta6-alpha7 loop into three different positions in the closed, intermediate, and open conformations, with a progressive increase in affinity.
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