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Article

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

Protein engineering, design & selection : PEDS - 1 May 2010

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

Abstract excerpt

Upon removal of the regulatory insert (RI), the first nucleotide binding domain (NBD1) of human cystic fibrosis transmembrane conductance regulator (CFTR) can be heterologously expressed and purified in a form that remains stable without solubilizing mutations, stabilizing agents or the regulatory extension (RE). This protein, NBD1 387-646(Delta405-436), crystallizes as a homodimer with a head-to-tail association...

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Source

Identifiers

PMID: 20150177
DOI: 10.1093/protein/gzq004

Genes

CFTR

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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