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Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins Piccard H; Van den Steen PE; Opdenakker GJ Leukoc Biol 2007[Apr]; 81 (4): 870-92The heme-binding hemopexin consists of two, four-bladed propeller domains connected by a linker region. Hemopexin domains are found in different species on the phylogenetic tree and in the human species represented in hemopexin, matrix metalloproteinases (MMPs), vitronectin, and products of the proteoglycan 4 gene. Hemopexin and hemopexin domains of human proteins fulfill functions in activation of MMPs, inhibition of MMPs, dimerization, binding of substrates or ligands, cleavage of substrates, and endocytosis by low-density lipoprotein receptor-related protein-1 (LRP-1; CD91) and LRP-2 (megalin, GP330). Insights into the structures and functions of hemopexin (domains) form the basis for positive or negative interference with the formation of molecular complexes and hence, might be exploited therapeutically in inflammation, cancer, and wound healing.|Amino Acid Sequence[MESH]|Dimerization[MESH]|Enzyme Activation[MESH]|Hemopexin/*chemistry/metabolism/physiology[MESH]|Humans[MESH]|Ligands[MESH]|Matrix Metalloproteinases/*chemistry/metabolism/physiology[MESH]|Models, Biological[MESH]|Molecular Sequence Data[MESH]|Protein Binding[MESH]|Protein Structure, Tertiary[MESH]|Sequence Homology, Amino Acid[MESH]|Structure-Activity Relationship[MESH] |
