The 1.25 Å resolution refinement of the cholera toxin B-pentamer: Evidence of peptide backbone strain at the receptor-binding site

Journal of Molecular Biology

Volumn 282, Issue 5, 1998, Pages 1043-1059

  Merritt, Ethan A ^a   Kuhn, Peter ^b   Sarfaty, Steve ^a   Erbe, Jarrod L ^c   Holmes, Randall K ^c   Hol, Wim G J ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^c UNIVERSITY OF COLORADO   (United States)

Author keywords

Anisotropic displacement parameters; Atomic resolution; Complex oligosaccharide; Crystal structure; SHELXL

Indexed keywords

CHOLERA TOXIN B SUBUNIT; CYSTEINE; GLUTAMINE; OLIGOSACCHARIDE; PEPTIDE; VALINE; CELL SURFACE RECEPTOR; CHOLERA TOXIN; CHOLERAGEN RECEPTOR; GANGLIOSIDE GM1; HYDROGEN; SOLVENT;

ACCURACY; ARTICLE; CRYSTAL STRUCTURE; DISULFIDE BOND; PRIORITY JOURNAL; RECEPTOR BINDING; REPRODUCIBILITY; TOXIN STRUCTURE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; METABOLISM; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CHOLERA TOXIN; CRYSTALLOGRAPHY, X-RAY; G(M1) GANGLIOSIDE; HYDROGEN; MODELS, MOLECULAR; PROTEIN CONFORMATION; RECEPTORS, CELL SURFACE; SOLVENTS;

EID: 0032500378     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2076     Document Type: Article

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