@article {528361,
	title = {Small molecule integrin antagonists that bind to the β2 subunit I-like domain and activate signals in one direction and block them in another},
	journal = {Immunity},
	volume = {19},
	number = {3},
	year = {2003},
	note = {in file},
	pages = {391-402},
	abstract = {Leukocyte integrins contain an inserted (I) domain in their alpha subunits and an I-like domain in their beta(2) subunit, which directly bind ligand and regulate ligand binding, respectively. We describe a novel mechanistic class of integrin inhibitors that bind to the metal ion-dependent adhesion site of the beta(2) I-like domain and prevent its interaction with and activation of the alpha(L) I domain. The inhibitors do not bind to the alpha(L) I domain but stabilize alpha/beta subunit association and can show selectivity for alpha(L)beta(2) compared to alpha(M)beta(2). The inhibitors reveal a crucial intersection for relaying conformational signals within integrin extracellular domains. While blocking signals in one direction to the I domain, the antagonists induce the active conformation of the I-like domain and stalk domains, and thus transmit conformational signals in the other direction toward the transmembrane domains.},
	author = {Shimaoka, M. and Salas, A. and Yang, W and Weitz-Schmidt, G. and Springer, T.A.}
}
