@article {546751,
	title = {Structural determinants of integrin β-subunit specificity for latent TGF-β.},
	journal = {Nat Struct Mol Biol.},
	volume = {21},
	number = {12},
	year = {2014},
	pages = {1091-6},
	abstract = {Eight\&nbsp;integrin\&nbsp;α-β heterodimers recognize ligands with an Arg-Gly-Asp (RGD) motif. However, the\&nbsp;structural\&nbsp;mechanism by which integrins differentiate among extracellular proteins with RGD motifs is not understood. Here, crystal structures, mutations and peptide-affinity measurements show that αVβ6 binds with high affinity to a RGDLXXL/I motif within the prodomains of TGF-β1 and TGF-β3. The LXXL/I motif forms an amphipathic α-helix that binds in a hydrophobic pocket in the β6 subunit. Elucidation of the basis for ligand binding\&nbsp;specificity\&nbsp;by the\&nbsp;integrin\&nbsp;β subunit reveals contributions by three different βI-domain loops, which we designatespecificity-determining loops (SDLs) 1, 2 and 3. Variation in a pair of single key residues in SDL1 and SDL3 correlates with the variation of the entire β subunit in\&nbsp;integrin\&nbsp;evolution, thus suggesting a paradigmatic role in overall β-subunit function.},
	author = {Dong, X. and Hudson, N.E. and Lu, C. and Springer, T.A.}
}
