Crystallographic and single-particle analyses of native- and nucleotide-bound forms of the cystic fibrosis transmembrane conductance regulator (CFTR) protein.

Abstract:

:Cystic fibrosis, one of the major human inherited diseases, is caused by defects in the CFTR (cystic fibrosis transmembrane conductance regulator), a cell-membrane protein. CFTR acts as a chloride channel which can be opened by ATP. Low-resolution structural studies of purified recombinant human CFTR are described in the present paper. Localization of the C-terminal decahistidine tag in CFTR was achieved by Ni2+-nitriloacetate nanogold labelling, followed by electron microscopy and single-particle analysis. The presence of the gold label appears to improve the single-particle-alignment procedure. Projection structures of CFTR from two-dimensional crystals analysed by electron crystallography displayed two alternative conformational states in the presence of nucleotide and nanogold, but only one form of the protein was observed in the quiescent (nucleotide-free) state.

journal_name

Biochem Soc Trans

authors

Awayn NH,Rosenberg MF,Kamis AB,Aleksandrov LA,Riordan JR,Ford RC

doi

10.1042/BST20050996

keywords:

subject

Has Abstract

pub_date

2005-11-01 00:00:00

pages

996-9

issue

Pt 5

eissn

0300-5127

issn

1470-8752

pii

BST20050996

journal_volume

33

pub_type

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