| 词条 | Hemopexin family |
| 释义 |
| Symbol = Hemopexin | Name = Hemopexin | image = | width = | caption = | Pfam= PF00045 | InterPro= IPR000585 | SMART= HX | Prosite = PDOC00023 | SCOP = 1hxn | TCDB = | OPM family= | OPM protein= | PDB= | Membranome family =536 }} The hemopexin family is a family of evolutionarily related proteins. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins).[1] The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs). Hemopexin ({{EC number|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.[2] 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,[3] 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.[4] 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). ExamplesHuman gene encoding proteins containing hemopexin-like repeats include:
References1. ^{{cite journal | author = Bode W | title = A helping hand for collagenases: the haemopexin-like domain | journal = Structure | volume = 3 | issue = 6 | pages = 527–30 |date=June 1995 | pmid = 8590012 | doi = 10.1016/s0969-2126(01)00185-x| url = | issn = }} {{InterPro content|IPR000585}}{{membrane-protein-stub}}2. ^{{cite journal |doi=10.1089/104454902753759717 |vauthors=Altruda F, Tolosano E |title=Hemopexin: structure, function, and regulation |journal=DNA Cell Biol. |volume=21 |issue=4 |pages=297–306 |year=2002 |pmid=12042069}} 3. ^{{cite journal |doi=10.1021/bi972247n |vauthors=Kojima K, Ogawa H, Matsumoto I, Yoneda A |title=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 |journal=Biochemistry |volume=37 |issue=18 |pages=6351–6360 |year=1998 |pmid=9572850}} 4. ^{{cite journal |doi=10.1023/A:1026093016148 |vauthors=Das S, Mandal M, Chakraborti T, Mandal A, Chakraborti S |title=Structure and evolutionary aspects of matrix metalloproteinases: a brief overview |journal=Mol. Cell. Biochem. |volume=253 |issue=1–2 |pages=31–40 |year=2003 |pmid=14619953}} 1 : Single-pass transmembrane proteins |
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