Member database | SUPERFAMILY |
SUPERFAMILY type | homologous superfamily |
Description Imported from IPR036375
Hemopexin (
3.2.1.35) is a serum glycoprotein that binds haem and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation
[1]. Hemopexin prevents haem-mediated oxidative stress. Structurally hemopexin consists of two similar halves of approximately two hundred amino acid residues connected by a histidine-rich hinge region. Each half is itself formed by the repetition of a basic unit of some 35 to 45 residues. Hemopexin-like domains have been found in two other types of proteins, vitronectin
[2], a cell adhesion and spreading factor found in plasma and tissues, and matrixins MMP-1, MMP-2, MMP-3, MMP-9, MMP-10, MMP-11, MMP-12, MMP-14, MMP-15 and MMP-16, members of the matrix metalloproteinase family that cleave extracellular matrix constituents
[3]. These zinc endopeptidases, which belong to MEROPS peptidase subfamily M10A, have a single hemopexin-like domain in their C-terminal section. It is suggested that the hemopexin domain facilitates binding to a variety of molecules and proteins, for example the HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).
References Imported from IPR036375
1.Hemopexin: structure, function, and regulation. Tolosano E, Altruda F. DNA Cell Biol. 21, 297-306, (2002). View articlePMID: 12042069
2.Characterization of the ligand binding activities of vitronectin: interaction of vitronectin with lipids and identification of the binding domains for various ligands using recombinant domains. Yoneda A, Ogawa H, Kojima K, Matsumoto I. Biochemistry 37, 6351-60, (1998). View articlePMID: 9572850
3.Structure and evolutionary aspects of matrix metalloproteinases: a brief overview. Das S, Mandal M, Chakraborti T, Mandal A, Chakraborti S. Mol. Cell. Biochem. 253, 31-40, (2003). View articlePMID: 14619953
Integrated to
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Representative structure
1itv: Dimeric form of the haemopexin domain of MMP9