Chemical shift assignments of the connexin45 carboxyl terminal domain: monomer and dimer conformations.
Chemical shift assignments of the connexin45 carboxyl terminal domain: monomer and dimer conformations.
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DOI：
10.1007/s12104-012-9431-9
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发表时间：
2013-10
影响因子：
0.9
通讯作者：
Sorgen PL
中科院分区：
文献类型：
--
作者：
Kopanic JL;Sorgen PL
Connexin45 (Cx45) is a gap junction protein involved in cell-to-cell communication in the heart and other tissues. Here we report the 1H, 15N, and 13C 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 α-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 α-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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DOI：
10.1159/000092560
发表时间：
2006-01-01
期刊：
CARDIOVASCULAR GAP JUNCTIONS
影响因子：
--
作者：
van Veen, Toon A. B.;van Rijen, Harold V. M.;Jongsina, Habo J.
通讯作者：
Jongsina, Habo J.
DOI：
10.1016/j.bbapap.2003.07.001
发表时间：
2003-12-01
影响因子：
3.2
作者：
Leach, RN;Boyett, MR;Findlay, JBC
通讯作者：
Findlay, JBC
影响因子：
2.7
作者：
DELAGLIO, F;GRZESIEK, S;BAX, A
通讯作者：
BAX, A
影响因子：
56.9
作者：
Unger, VM;Kumar, NM;Yeager, M
通讯作者：
Yeager, M
影响因子：
2.7
作者：
JOHNSON, BA;BLEVINS, RA
通讯作者：
BLEVINS, RA