The col-1 module of human matrix metalloproteinase-2 (MMP-2): Structural/functional relatedness between gelatin-binding fibronectin type II modules and lysine-binding kringle domains

Biological Chemistry

Volumn 383, Issue 1, 2002, Pages 137-148

  Gehrmann, Marion ^a   Briknarová, Klára ^a   Bányai, László ^a   Patthy, László ^a   Llinás, Miguel ^a  

^a CARNEGIE MELLON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; AROMATIC AMINO ACID; CYSTEINE; FIBRONECTIN; GELATIN; GELATINASE A; GLYCINE; LYSINE; PROLINE; COL 1 PEPTIDE, HUMAN; COL-1 PEPTIDE, HUMAN; PEPTIDE FRAGMENT;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; BINDING SITE; CHEMICAL BOND; CONTROLLED STUDY; HUMAN; HYDROPHOBICITY; KRINGLE DOMAIN; MOLECULAR MIMICRY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; CHEMISTRY; CONSENSUS SEQUENCE; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; BINDING SITES; CONSENSUS SEQUENCE; FIBRONECTINS; GELATIN; HUMANS; KRINGLES; LYSINE; MATRIX METALLOPROTEINASE 2; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; REPETITIVE SEQUENCES, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0036005968     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2002.014     Document Type: Article

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