Protein-protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces

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

Volumn 100, Issue 10, 2003, Pages 5772-5777

  Ma, Buyong ^a   Elkayam, Tal ^b   Wolfson, Haim ^b   Nussinov, Ruth ^a,b  

^a NATIONAL CANCER INSTITUTE   (United States)

^b TEL AVIV UNIVERSITY   (Israel)

Author keywords

Binding site prediction; Hot spots; Molecular recognition; Protein protein interfaces; Residue conservation

Indexed keywords

ARTICLE; BINDING SITE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; GENETIC CONSERVATION; HYDROGEN BOND; HYDROPHOBICITY; MACROMOLECULE; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RESIDUE ANALYSIS; STRUCTURE ANALYSIS; SURFACE PROPERTY; TISSUE SPECIFICITY;

AMINO ACID SEQUENCE; BINDING SITES; CONSERVED SEQUENCE; EPITOPES; MOLECULAR SEQUENCE DATA; PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; TRYPTOPHAN;

EID: 0037609791     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.1030237100     Document Type: Article

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