CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices-Reference-Cited by-同舟云学术

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CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices

Published:2007-07-29 Issue:8 Volume:14 Page:738-745
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Baker Jennifer M R,Hudson Rhea P,Kanelis Voula,Choy Wing-Yiu,Thibodeau Patrick H,Thomas Philip J,Forman-Kay Julie D

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb1278.pdf

Reference50 articles.

1. Riordan, J.R. et al. Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science 245, 1066–1072 (1989).

2. Dawson, R.J. & Locher, K.P. Structure of a bacterial multidrug ABC transporter. Nature 443, 180–185 (2006).

3. Ostedgaard, L.S., Baldursson, O., Vermeer, D.W., Welsh, M.J. & Robertson, A.D. A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution. Proc. Natl. Acad. Sci. USA 97, 5657–5662 (2000).

4. Dulhanty, A.M. & Riordan, J.R. Phosphorylation by cAMP-dependent protein kinase causes a conformational change in the R domain of the cystic fibrosis transmembrane conductance regulator. Biochemistry 33, 4072–4079 (1994).

5. Smith, P.C. et al. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139–149 (2002).

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