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Structural insights into the mechanical regulation of molecular recognition sites

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TRENDS IN BIOTECHNOLOGY
卷 19, 期 10, 页码 416-+

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ELSEVIER SCIENCE LONDON
DOI: 10.1016/S0167-7799(01)01737-1

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  1. NIGMS NIH HHS [R01 GM49063, 5 T32 GM08268] Funding Source: Medline

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Intriguing experimental and computational data are emerging to suggest that mechanical forces regulate the functional states of some proteins by stretching them into nonequilibrium states. Using the, extracellular matrix protein fibronectin as an: example, we discuss molecular design principles that might control the exposure of a protein's recognition sites, and/or their relative distances, in a force-dependent manner. Fibronectin, regulates many cellular functions by, binding directly to, integrins. Although integrins have a key role in the transduction of force across the cell, membrane by coupling the extracellular matrix to the cytoskeleton, the studies reviewed here suggest that fibronectin might be one of the molecules responsible for the initial transformation. of mechanical force into a biochemical. signal.

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