TY - JOUR
T1 - 1H, 13C, and 15N backbone resonance assignments of the connexin43 carboxyl terminal domain attached to the 4th transmembrane domain in detergent micelles
AU - Grosely, Rosslyn
AU - Kieken, Fabien
AU - Sorgen, Paul L.
N1 - Funding Information:
Acknowledgments This work is funded by the United States Public Health Service Grant, GM072631. Rosslyn Grosely is funded by the Graduate Assistance in Areas of National Need (GAANN) Fellowship, McDonald Fellowship, Regents Tuitions Fellowship, and the Fred W. Upson Grant. We would like to acknowledge Dr. Asokan Anbanandam for his assistance in collecting data at the University of Kansas NIH Center of Biomedical Research Excellence in Protein Structure and Function, which is supported by NIH grant RR-017708; Ed Ezell, who manages the NMR facility at the University of Nebraska Medical Center; and Jeff Lovelace for his heroic efforts in our computer lab.
PY - 2013/10
Y1 - 2013/10
N2 - Gap junctions are specialized membrane channels that enable coordination of cellular functions and whole-organ responses by facilitating both molecular and electrical communication between neighboring cells. Connexin43 (Cx43) is the most widely expressed and well-studied gap junction protein. In the heart, Cx43 is essential for normal cardiac development and function. Studies using a soluble version of the Cx43 carboxyl-terminal domain (Cx43CT; S255-I382) have established the central role it plays in channel regulation. However, in purifying and characterizing a more 'native-like' construct (Cx43CT attached to the fourth transmembrane domain (TM4-Cx43CT; D196-I382)), we have identified that the TM4-Cx43CT is a better model than the soluble Cx43CT to further investigate the mechanisms governing Cx43 channel regulation. Here, we report the backbone 1H, 15N, and 13C assignments and predicted secondary structure of the TM4-Cx43CT. Assignment of the TM4-Cx43CT is a key step towards a better understanding of the structural basis of Cx43 regulation, which will lead to improved strategies for modulation of junctional communication that has been altered due to disease or ischemic injury.
AB - Gap junctions are specialized membrane channels that enable coordination of cellular functions and whole-organ responses by facilitating both molecular and electrical communication between neighboring cells. Connexin43 (Cx43) is the most widely expressed and well-studied gap junction protein. In the heart, Cx43 is essential for normal cardiac development and function. Studies using a soluble version of the Cx43 carboxyl-terminal domain (Cx43CT; S255-I382) have established the central role it plays in channel regulation. However, in purifying and characterizing a more 'native-like' construct (Cx43CT attached to the fourth transmembrane domain (TM4-Cx43CT; D196-I382)), we have identified that the TM4-Cx43CT is a better model than the soluble Cx43CT to further investigate the mechanisms governing Cx43 channel regulation. Here, we report the backbone 1H, 15N, and 13C assignments and predicted secondary structure of the TM4-Cx43CT. Assignment of the TM4-Cx43CT is a key step towards a better understanding of the structural basis of Cx43 regulation, which will lead to improved strategies for modulation of junctional communication that has been altered due to disease or ischemic injury.
KW - Cx43
KW - Gap junction
KW - Intrinsically disordered protein
KW - LPPG detergent micelles
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U2 - 10.1007/s12104-012-9432-8
DO - 10.1007/s12104-012-9432-8
M3 - Article
C2 - 23065337
AN - SCOPUS:84883487108
SN - 1874-2718
VL - 7
SP - 299
EP - 303
JO - Biomolecular NMR Assignments
JF - Biomolecular NMR Assignments
IS - 2
ER -