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- W1966781861 abstract "Integrin-dependent adhesion and signaling are regulated by conformational changes whose details remain controversial. Crystallography revealed bent shapes for resting and primed integrin ectodomains, whereas large, ligand-induced rearrangements in other constructs suggested extension, “opening,” and tail separation. We have used experimental/computed hydrodynamics to discriminate among different αvβ3 and αIIbβ3 atomic models built on X-ray, NMR, and EM data. In contrast with X-ray structures and EM maps, hydrodynamics indicate that resting integrins are already extended. Furthermore, the hydrodynamics of an αvβ3 ectodomain-fibronectin fragment complex support opening via additional head region conformational changes (hybrid domain swing-out), but without tail separation. Likewise, frictional changes induced by priming agents in full-length αIIbβ3 correlate well with the swing-out coupled to a simple transmembrane helix shift in an extended, electron tomography-based model. Extension and immediate tail separation are then uncoupled from head region rearrangements following activation, thus underscoring integrins' delicate, finely tuned plasticity." @default.
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- W1966781861 date "2008-06-01" @default.
- W1966781861 modified "2023-09-30" @default.
- W1966781861 title "Integrin Conformational Regulation: Uncoupling Extension/Tail Separation from Changes in the Head Region by a Multiresolution Approach" @default.
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- W1966781861 doi "https://doi.org/10.1016/j.str.2008.02.019" @default.
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