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Integrin Structure, Activation, and Interactions
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DOI：10.1101/cshperspect.a004994.png)
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Abstract
En 中文
Integrins are large, membrane-spanning, heterodimeric proteins that are essential for a metazoan existence. All members of the integrin family adopt a shape that resembles a large head on two legs, with the head containing the sites for ligand binding and subunit association. Most of the receptor dimer is extracellular, but both subunits traverse the plasma membrane and terminate in short cytoplasmic domains. These domains initiate the assembly of large signaling complexes and thereby bridge the extracellular matrix to the intracellular cytoskeleton. To allow cells to sample and respond to a dynamic pericellular environment, integrins have evolved a highly responsive receptor activation mechanism that is regulated primarily by changes in tertiary and quaternary structure. This review summarizes recent progress in the structural and molecular functional studies of this important class of adhesion receptor.
Keywords:
I-LIKE DOMAIN
CRYSTAL-STRUCTURE
A-DOMAIN
MONOCLONAL-ANTIBODIES
CONFORMATIONAL-CHANGES
EXTRACELLULAR SEGMENT
CYTOPLASMIC DOMAINS
LIGAND-BINDING
TRANSMEMBRANE
COMPLEX
Journal
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10.1
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3.0K
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