Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 7, Issue 2, Pages 293-297Publisher
SPRINGER
DOI: 10.1007/s12104-012-9431-9
Keywords
Cx45; Gap junction; Dimerization; Carboxyl terminus; Intrinsically disordered protein
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Funding
- United States Public Health Sevice Grant [GM072631]
- Graduate Assistance in Areas of National Need (GAANN) Fellowship
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Connexin45 (Cx45) is a gap junction protein involved in cell-to-cell communication in the heart and other tissues. Here we report the H-1, N-15, and C-13 resonance assignments for the monomer and dimer conformations of the Cx45 carboxyl terminal (Cx45CT) domain and provide evidence of dimerization using diffusion ordered spectroscopy. The predicted secondary structure of the Cx45CT domain based on the chemical shifts identified one region of alpha-helical structure, which corresponds to the residues that broadened beyond detection in the dimer confirmation. Previous biophysical studies from our laboratory characterizing the CT domain from the other major cardiac connexins, Cx40 and Cx43, suggest that the amount of alpha-helical content may translate into the ability of a protein to dimerize. Even though the CT domain is thought to be the main regulatory domain of most connexins, the physiological role of CT dimerization is currently unknown. Therefore, these assignments will be useful for determining the intermolecular interactions that mediate Cx45CT dimerization, information that will be used to characterize dimerization in functional channels, as well as characterizing the binding sites for molecular partners involved in Cx45 regulation.
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