期刊
CELL
卷 110, 期 5, 页码 599-611出版社
CELL PRESS
DOI: 10.1016/S0092-8674(02)00935-2
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资金
- NHLBI NIH HHS [HL48675] Funding Source: Medline
- NIGMS NIH HHS [GM62580] Funding Source: Medline
How ligand binding alters integrin conformation in outside-in signaling, and how inside-out signals alter integrin affinity for ligand, have been mysterious. We address this with electron microscopy, physicochemical measurements, mutational introduction of disulfides, and ligand binding to alphaVbeta3 and alphaIIbbeta3 integrins. We show that a highly bent integrin conformation is physiological and has low affinity for biological ligands. Addition of a high affinity ligand mimetic peptide or Mn2+ results in a switch blade-like opening to an extended structure. An outward swing of the hybrid domain at its junction with the I-like domain shows conformational change within the headpiece that is linked to ligand binding. Breakage of a C-terminal clasp between the alpha and beta subunits enhances Mn2+ induced unbending and ligand binding.
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