Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?

Protein Science

Volumn 13, Issue 1, 2004, Pages 190-202

  Caffrey, Daniel R ^a   Somaroo, Shyamal ^a   Hughes, Jason D ^a   Mintseris, Julian ^b   Huang, Enoch S ^a  

^a PFIZER INC   (United States)

^b Boston University   (United States)

Author keywords

Binding; Evolution; Interactions; Protein structure; Sequence conservation

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVE SITE; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; AMINO ACIDS; BINDING SITES; CLUSTER ANALYSIS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DATABASES, FACTUAL; DIMERIZATION; ENTROPY; ENZYMES; EVOLUTION, MOLECULAR; GENOMICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SOLVENTS; SURFACE PROPERTIES;

EID: 0346733329     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03323604     Document Type: Article

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