Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant-Reference-Cited by-同舟云学术

Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant

Published:2010-02-11 Issue:5 Volume:23 Page:375-384
ISSN:1741-0134
Container-title:Protein Engineering, Design and Selection
language:en
Short-container-title:

Author:

Atwell Shane,Brouillette Christie G.,Conners Kris,Emtage Spencer,Gheyi Tarun,Guggino William B.,Hendle Jorg,Hunt John F.,Lewis Hal A.,Lu Frances,Protasevich Irina I.,Rodgers Logan A.,Romero Rich,Wasserman Stephen R.,Weber Patricia C.,Wetmore Diana,Zhang Feiyu F.,Zhao Xun

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/23/5/375/17494208/gzq004.pdf

Reference46 articles.

1. The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover

2. Structure of P-Glycoprotein Reveals a Molecular Basis for Poly-Specific Drug Binding

3. CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices

4. The CCP4 suite: programs for protein crystallography

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