Structural organization of gap junction channels

Gina E. Sosinsky, Bruce J. Nicholson

Research output: Contribution to journalReview articlepeer-review

183 Scopus citations

Abstract

Gap junctions were initially described morphologically, and identified as semi-crystalline arrays of channels linking two cells. This suggested that they may represent an amenable target for electron and X-ray crystallographic studies in much the same way that bacteriorhodopsin has. Over 30 years later, however, an atomic resolution structural solution of these unique intercellular pores is still lacking due to many challenges faced in obtaining high expression levels and purification of these structures. A variety of microscopic techniques, as well as NMR structure determination of fragments of the protein, have now provided clearer and correlated views of how these structures are assembled and function as intercellular conduits. As a complement to these structural approaches, a variety of mutagenic studies linking structure and function have now allowed molecular details to be superimposed on these lower resolution structures, so that a clearer image of pore architecture and its modes of regulation are beginning to emerge.

Original languageEnglish (US)
Pages (from-to)99-125
Number of pages27
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1711
Issue number2 SPEC. ISS.
DOIs
StatePublished - Jun 10 2005

Keywords

  • Atomic force microscopy
  • Connexin
  • Electron microscopy
  • Gap junction
  • Gating
  • Mutagenesis
  • NMR
  • Pore structure
  • Structure

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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