The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding

Protein Science

Volumn 6, Issue 6, 1997, Pages 1148-1156

  Guddat, Luke W ^a   Bardwell, James C A ^b   Zander, Thomas ^b   Martin, Jennifer L ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b UNIVERSITY OF MICHIGAN   (United States)

Author keywords

DsbA; Oxidoreductase; Peptide interaction; Protein crystallography; Protein disulfide isomerase; Thioredoxin fold

Indexed keywords

BACTERIAL PROTEIN; DISULFIDE; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; THIOREDOXIN;

ARTICLE; CRYSTAL STRUCTURE; DISULFIDE BOND; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0031010755     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060603     Document Type: Article

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