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| 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 |
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| Author(s): BODE W, GOMISRUTH FX, STOCKLER W |
| Source: FEBS LETTERS Volume: 331 Issue: 1-2 Pages: 134-140 Published: SEP 27 1993 |
| Times Cited: 372 References: 31 |
| Abstract: The X-ray crystal structures of two zinc endopeptidases, astacin from crayfish, and adamalysin II from snake venom, reveal a strong overall topological equivalence and virtually identical extended HEXXHXXGXXH zinc-binding segments, but in addition a methionine-containing turn of similar conformation (the 'Met-tum'), which forms a hydrophobic basis for the zinc ion and the three liganding histidine residues. These two features are also present in a similar arrangement in the matrix metalloproteinases (matrixins) and in the large bacterial Serratia proteinase-like peptidases (serralysins). We suggest that these four proteinases represent members of distinct subfamilies which can be grouped together in a family, for which we propose the designation, metzincins. |
| Document Type: Article |
| Language: English |
| Reprint Address: BODE, W (reprint author), MAX PLANCK INST BIOCHEM, STRUKTURFORSCH ABT, D-82152 MARTINSRIED, GERMANY |
Addresses:
1. UNIV AUTONOMA BARCELONA, INST BIOL FONAMENTAL, E-08193 BARCELONA, SPAIN
2. UNIV HEIDELBERG, FACHRICHTUNG PHYSIOL, INST ZOOL, D-69120 HEIDELBERG, GERMANY |
| Publisher: ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: LZ251 |
| ISSN: 0014-5793 |
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