Cystic fibrosis: Recent structural insights

Michael Dorwart, Patrick Thibodeau, Philip Thomas

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

Cystic fibrosis (CF) is a debilitating human disease caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. The recently solved crystal structures of the murine CFTR nucleotide binding domain (NBD) provide insight into the molecular basis of several CF-causing mutations. In addition, the NBD structures reveal several unexpected findings that may have implications concerning CFTR function. In this mini-review, we discuss the key structural features of ATP Binding Cassette (ABC) transporter NBDs, as well as highlight how structural information has aided our understanding of the ATP-regulated solute transport cycle.

Original languageEnglish (US)
Pages (from-to)91-94
Number of pages4
JournalJournal of Cystic Fibrosis
Volume3
Issue numberSUPPL. 2
DOIs
StatePublished - Aug 2004

    Fingerprint

Keywords

  • ABC
  • CFTR
  • Cystic fibrosis
  • F508
  • NBD
  • Transporter

ASJC Scopus subject areas

  • Pediatrics, Perinatology, and Child Health
  • Pulmonary and Respiratory Medicine

Cite this