PMID:9687375

Citation	Baldwin, ET, Sarver, RW, Bryant, GL Jr, Curry, KA, Fairbanks, MB, Finzel, BC, Garlick, RL, Heinrikson, RL, Horton, NC, Kelley, LL, Mildner, AM, Moon, JB, Mott, JE, Mutchler, VT, Tomich, CS, Watenpaugh, KD and Wiley, VH (1998) Cation binding to the integrin CD11b I domain and activation model assessment. Structure 6:923-35
Abstract	The integrin family of cell-surface receptors mediate cell adhesion through interactions with the extracellular matrix or other cell-surface receptors. The alpha chain of some integrin heterodimers includes an inserted 'I domain' of about 200 amino acids which binds divalent metal ions and is essential for integrin function. Lee et al. proposed that the I domain of the integrin CD11b adopts a unique 'active' conformation when bound to its counter receptor. In addition, they proposed that the lack of adhesion in the presence of Ca2+ ion reflected the stabilization of an 'inactive' I-domain conformation. We set out to independently determine the structure of the CD11 b I domain and to evaluate the structural effects of divalent ion binding to this protein.
Links	PubMed
Keywords	Amino Acid Sequence; Binding Sites; Cadmium/chemistry; Cadmium/metabolism; Cations; Crystallography, X-Ray; Macrophage-1 Antigen/chemistry; Macrophage-1 Antigen/metabolism; Magnesium/chemistry; Magnesium/metabolism; Manganese/chemistry; Manganese/metabolism; Metals/chemistry; Metals/metabolism; Models, Molecular; Protein Conformation
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