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Papers In Press, published online ahead of print December 1, 2004
J. Biol. Chem, 10.1074/jbc.M411515200
Submitted on October 8, 2004
Revised on November 26, 2004
Accepted on December 1, 2004

Structural and biochemical characterization of CIB1 delineates a new family of EF-hand containing proteins

Holly R. Gentry, Alex U. Singer, Laurie Betts, Cheng Yang, Joseph D. Ferrara, John Sondek, and Leslie V. Parise

Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7365

Corresponding Author: sondek{at}med.unc.edu

CIB1 (CIB) is an EF-hand containing protein that binds multiple effector proteins including the platelet {a}IIb{b}3 integrin and several serine/threonine kinases and potentially modulates their function. The crystal structure for Ca2+-bound CIB1 has been determined at 2.0 Å resolution and reveals a compact {a}-helical protein containing four EF-hands, the last two of which bind calcium ions in the standard fashion seen in many other EF-hand proteins. CIB1 shares high structural similarity with calcineurin B and the neuronal calcium sensor (NCS) family of EF-hand containing proteins. Most importantly, like calcineurin B and NCS proteins, which possess a large hydrophobic pocket necessary for ligand binding, CIB1 contains a hydrophobic pocket that has been implicated in ligand binding by previous mutational analysis. However, unlike several NCS proteins, Ca2+-bound CIB1 is largely monomeric whether bound to a relevant peptide ligand or ligand-free. Differences in structure, oligomeric state, and phylogeny define a new family of CIB1-related proteins that extends from arthropods to humans.


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