@article {530246,
	title = {Structural basis of activation-dependent binding of ligand-mimetic antibody AL-57 to integrin LFA-1},
	journal = {Proc Natl Acad Sci USA},
	volume = {106},
	number = {43},
	year = {2009},
	note = {Zhang, HongminLiu, Jin-HuanYang, WeiSpringer, TimothyShimaoka, MotomuWang, Jia-HuaiAI063421/AI/NIAID NIH HHS/United StatesCA31798/CA/NCI NIH HHS/United StatesHL48675/HL/NHLBI NIH HHS/United StatesResearch Support, N.I.H., ExtramuralUnited StatesProceedings of the National Academy of Sciences of the United States of AmericaProc Natl Acad Sci U S A. 2009 Oct 27;106(43):18345-50. Epub 2009 Sep 23.},
	month = {Oct 27},
	pages = {18345-50},
	edition = {2009/10/07},
	abstract = {The activity of integrin LFA-1 (alpha(L)beta(2)) to its ligand ICAM-1 is regulated through the conformational changes of its ligand-binding domain, the I domain of alpha(L) chain, from an inactive, low-affinity closed form (LA), to an intermediate-affinity form (IA), and then finally, to a high-affinity open form (HA). A ligand-mimetic human monoclonal antibody AL-57 (activated LFA-1 clone 57) was identified by phage display to specifically recognize the affinity-upregulated I domain. Here, we describe the crystal structures of the Fab fragment of AL-57 in complex with IA, as well as in its unligated form. We discuss the structural features conferring AL-57{\textquoteright}s strong selectivity for the high affinity, open conformation of the I domain. The AL-57-binding site overlaps the ICAM-1 binding site on the I domain. Furthermore, an antibody Asp mimics an ICAM Glu by forming a coordination to the metal-ion dependent adhesion site (MIDAS). The structure also reveals better shape complementarity and a more hydrophobic interacting interface in AL-57 binding than in ICAM-1 binding. The results explain AL-57{\textquoteright}s antagonistic mimicry of LFA-1{\textquoteright}s natural ligands, the ICAM molecules.},
	isbn = {1091-6490 (Electronic)},
	author = {Zhang, H and Liu, J-H. and Yang, W and Springer, T. and Shimaoka, M. and J.-H. Wang}
}
