Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 7, Issue 2, Pages 299-303Publisher
SPRINGER
DOI: 10.1007/s12104-012-9432-8
Keywords
Cx43; Gap junction; LPPG detergent micelles; Intrinsically disordered protein
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Funding
- United States Public Health Service Grant [GM072631]
- Graduate Assistance in Areas of National Need (GAANN) Fellowship
- McDonald Fellowship
- Regents Tuitions Fellowship
- Fred W. Upson Grant
- NIH [RR-017708]
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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 H-1, N-15, and C-13 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.
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