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Article

Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry.

Journal of molecular biology - 19 Feb 2010

Lewis H A, Wang C, Zhao X, Hamuro Y, Conners K, Kearins M C, Lu F, Sauder J M, Molnar K S, Coales S J, Maloney P C, Guggino W B, Wetmore D R, Weber P C, Hunt J F

Abstract excerpt

The DeltaF508 mutation in nucleotide-binding domain 1 (NBD1) of the cystic fibrosis transmembrane conductance regulator (CFTR) is the predominant cause of cystic fibrosis. Previous biophysical studies on human F508 and DeltaF508 domains showed only local structural changes restricted to residues...

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Share to Cystic Fibrosis
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Interaction Domains and Motifs

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Source

Identifiers

PMID: 19944699
DOI: 10.1016/j.jmb.2009.11.051

Genes

CFTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19944699-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry.PMID 19944699Read ↗

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