Tissue inhibitors of metalloproteinases (TIMP) are a family of proteins that can form complexes with extracellular matrix metalloproteinases (suchas collagenases) and irreversibly inactivate them. TIMP's are proteins ofabout 200 amino acid residues, 12 of which are cysteines involved in disulfidebonds. The basic structure of such a type of inhibitor is shown in thefollowing schematic representation: +-----------------------------+ +--------------+ **|** | | | CxCxCxxxxxxxxxxxxxxxxxCxxxxxxxxxCxxxxxxxCxCxCxCxCxxxxxCxxCxxx | | | | | | | | | +-----------------|-----------------+ +-+ +-----+ +---------------------+'C': conserved cysteine involved in a disulfide bond.This conserved site is found at the N-terminal extremity of theseproteins, which includes three conserved cysteines.