1H, 13C, and 15N backbone resonance assignments of the connexin43 carboxyl terminal domain attached to the 4th transmembrane domain in detergent micelles

Rosslyn Grosely, Fabien Kieken, Paul L. Sorgen

Research output: Contribution to journalArticle

4 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)299-303
Number of pages5
JournalBiomolecular NMR Assignments
Issue number2
StatePublished - Oct 1 2013



  • Cx43
  • Gap junction
  • Intrinsically disordered protein
  • LPPG detergent micelles

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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