Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'

FEBS Letters

Volumn 331, Issue 1-2, 1993, Pages 134-140

  Bode, Wolfram ^a   Gomis Rüth, Franz Xaver ^b   Stöckler, Walter ^c  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

^c UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

Astacin: Snake venom metalloproteinase; Matrix metalloproteinase; Protein crystal structure; Thermolysin; Zinc endopeptidase family

Indexed keywords

ASTACENE; METALLOPROTEINASE; SERRALYSIN; SNAKE VENOM; UNCLASSIFIED DRUG; ZINC;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ANIMAL; BINDING SITES; ENDOPEPTIDASES; EXTRACELLULAR MATRIX; HUMAN; METALLOENDOPEPTIDASES; METHIONINE; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SERRATIA; SNAKE VENOMS; SUPPORT, NON-U.S. GOV'T; ZINC;

EID: 0027515396     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(93)80312-I     Document Type: Article

References (31)

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5. Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif.
6. Proteins
7. RIBBON: a stereo cartoon drawing program for proteins