Metal-binding loop length and not sequence dictates structure

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 14, 2009, Pages 5616-5621

  Sato, Katsuko ^a   Li, Chan ^a   Salard, Isabelle ^a   Thompson, Andrew J ^a   Banfield, Mark J ^b   Dennison, Christopher ^a  

^a NEWCASTLE UNIVERSITY   (United Kingdom)

^b JOHN INNES CENTRE   (United Kingdom)

Author keywords

Loop modeling; Metalloproteins; Protein engineering protein folding; Strand swapped dimerization

Indexed keywords

ALANINE; COPPER; COPPER DERIVATIVE; CUPREDOXIN AZURIN; CYSTEINE; GLYCINE; HISTIDINE; METHIONINE; METHYL GROUP; UNCLASSIFIED DRUG; VALINE;

AMINO ACID COMPOSITION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; METAL BINDING; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN ISOLATION; SEQUENCE ANALYSIS; SPECTROSCOPY; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; AMINO ACIDS; AZURIN; BACTERIAL PROTEINS; BINDING SITES; COPPER; PROTEIN CONFORMATION;

EID: 65249101343     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0811324106     Document Type: Article

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