期刊
BIOPHYSICAL CHEMISTRY
卷 144, 期 3, 页码 130-135出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bpc.2009.08.001
关键词
Calmodulin; Gap junction; Connexin43; Solution structure; Calorimetry; Regulation
资金
- Academy of Finland
- Sigrid Juselius Foundation
- Department of Biochemistry
- University of Oulu
- European Community [R113-CT-2004-506008]
Gap junctions are formed by a family of transmembrane proteins, connexins. Connexin43 is a widely studied member of the family, being ubiquitously expressed in a variety of tissues and a target of a large number of disease mutations. The intracellular loop of connexin43 has been shown to include a calmodulin binding domain, but detailed 3-dimensional data on the structure of the complex are not available. In this study, we used a synthetic peptide from this domain to reveal the conformation of the calmodulin-peptide complex by small angle X-ray scattering. Upon peptide binding, calmodulin lost its dumbbell shape, adopting a more globular conformation. We also studied the energetics of the interaction using calorimetry and computational methods. All our data indicate that calmodulin binds to the peptide from cx43 in the classical 'collapsed' conformation. (C) 2009 Elsevier B.V. All rights reserved.
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