Integrins structures

Luo B, Springer TA. 2006. Integrin structures and conformational signaling. Curr Opin Cell Biol. 18 1-8. 

DeSimone DW, Hynes RO. Xenopus laevie integrins. Structural conservation and evolutionary divergence of integrin beta. J Biol Chem 1988 263(1 l) 5333 5340. 

Kramer, R. H., Enenstein, J., and Waleh, N. S., Integrin structure and ligand specificity in cell-matrix interactions, in Molecular and Cellular Aspects of Basement Membranes (D. H. Rohrbach and R. Timpl, Eds.), pp. 239-258. Academic Press, New York, 1993. 

Mechanosensing is postulated to involve many different cellular and extracellular components. Mechanical forces cause direct stretching of protein-cell surface integrin binding sites that occur on all eukaryotic cells. Stress-induced conformational changes in the extracellular matrix may alter integrin structure and lead to activation of several secondary messenger pathways within the cell. Activation of these pathways leads to altered reg-... 

Small molecule antagonists have been used to obtain important insights into the conformational regulation of integrin structure and function (Shimaoka and Springer, 2003). The ability of ligands and ligand-mimetic... 

Shimaoka, M., Takagi, J., and Springer, T. A. (2002). Conformational regulation of integrin structure and function. Anna. Rev. Biophys. Biomol. Struct. 31, 485—516. 

DeSimoie DW, Hynes RO Xenopus laevis integrins. Structural conservation and evoluti< ary divergoice of integrin b subunits. J Biol Chem 263 5333-5340,1988. 

The Rho family of small GTP-binding proteins functions to regulate the assembly of distinct actin structures in cells Rho regulates stress fiber assembly, Rac regulates lamellipodia protrusion and Cdc42 stimulates protrusion of the plasma membrane to form filopodia (Ridley and Hall, 1992 Ridley et at., 1992 Nobes and Hall, 1995 Kozma et at., 1995). All three regulate attachment of cells to the extracellular matrix via adhesive integrin structures (Nobes and Hall, 1995). 

A FIGURE 6-25 Model of fibronectin binding to integrin through its RGD-containing type III repeat, (a) Scale model of fibronectin Is shown docked by two type III repeats to the extracellular domains of Integrin. Structures of fibronectin s domains were determined from fragments of the molecule. 

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