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PROSITE documentation PDOC00260 [for PROSITE entry PS00288]

Tissue inhibitors of metalloproteinases signature


Tissue inhibitors of metalloproteinases (TIMP) are a family of proteins [1,2,3] that can form complexes with extracellular matrix metalloproteinases (such as collagenases) and irreversibly inactivate them. TIMP's are proteins of about 200 amino acid residues, 12 of which are cysteines involved in disulfide bonds [4]. The basic structure of such a type of inhibitor is shown in the following schematic representation:

          +-----------------------------+         +--------------+
        **|**                           |         |              |
        |   |                 |                 |   | | |     |
        |   +-----------------|-----------------+   +-+ +-----+
'C': conserved cysteine involved in a disulfide bond.
'*': position of the pattern.

As a signature pattern for TIMP's, we chose the N-terminal extremity of these proteins, which includes three conserved cysteines.

Last update:

May 2004 / Text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

TIMP, PS00288; Tissue inhibitors of metalloproteinases signature  (PATTERN)


1AuthorsStetler-Stevenson W.G. Krutzsch H.C. Liotta L.A.
SourceJ. Biol. Chem. 264:17374-17378(1989).

2AuthorsWoessner J.F. Jr.
TitleMatrix metalloproteinases and their inhibitors in connective tissue remodeling.
SourceFASEB J. 5:2145-2154(1991).
PubMed ID1850705

3AuthorsPavloff N. Staskus P.W. Kishnani N.S. Hawkes S.P.
TitleA new inhibitor of metalloproteinases from chicken: ChIMP-3. A third member of the TIMP family.
SourceJ. Biol. Chem. 267:17321-17326(1992).
PubMed ID1512267

4AuthorsWilliamson R.A. Marston F.A.O. Angal S. Koklitis P. Panico M. Morris H.R. Carne A.F. Smith B.J. Harris T.J.R. Freedman R.B.
TitleDisulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP).
SourceBiochem. J. 268:267-274(1990).
PubMed ID2163605

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