Introduction to section IV: biophysical methods to approach CFTR structure.

Juan L. Mendoza, André Schmidt, Philip J. Thomas

Research output: Contribution to journalEditorial

2 Scopus citations

Abstract

Inefficient folding of CFTR into a functional three-dimensional structure is the basic pathophysiologic mechanism leading to most cases of cystic fibrosis. Knowledge of the structure of CFTR and placement of these mutations into a structural context would provide information key for developing targeted therapeutic approaches for cystic fibrosis. As a large polytopic membrane protein containing disordered regions, intact CFTR has been refractory to efforts to solve a high-resolution structure using X-ray crystallography. The following chapters summarize current efforts to circumvent these obstacles by utilizing NMR, electron microscopy, and computational methodologies and by development of experimental models of the relevant domains of CFTR.

Original languageEnglish (US)
Pages (from-to)321-327
Number of pages7
JournalMethods in molecular biology (Clifton, N.J.)
Volume741
DOIs
StatePublished - Sep 7 2011

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ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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