Search results for "MATH domain"

showing 2 items of 2 documents

Meprins, membrane-bound and secreted astacin metalloproteinases

2008

The astacins are a subfamily of the metzincin superfamily of metalloproteinases. The first to be characterized was the crayfish enzyme astacin. To date more than 200 members of this family have been identified in species ranging from bacteria to humans. Astacins are involved in developmental morphogenesis, matrix assembly, tissue differentiation and digestion. Family members include the procollagen C-proteinase (BMP1, bone morphogenetic protein 1), tolloid and mammalian tolloid-like, HMP (Hydra vulgaris metalloproteinase), sea urchin BP10 (blastula protein) and SPAN (Strongylocentrotus purpuratus astacin), the 'hatching' subfamily comprising alveolin, ovastacin, LCE, HCE ('low' and 'high' c…

Models MolecularSubfamilyanimal structuresProtein ConformationClinical BiochemistryMolecular Sequence DataMatrix metalloproteinaseBiochemistryBone morphogenetic protein 1ArticleSubstrate SpecificityExtracellular matrixIntestinal mucosaAnimalsHumansTissue DistributionAmino Acid SequenceIntestinal MucosaMolecular BiologyPhylogenybiologyMetalloendopeptidasesGeneral Medicinebiology.organism_classificationStrongylocentrotus purpuratusMolecular biologyCell biologyProtein Subunitsembryonic structuresMolecular MedicineMATH domainAstacin
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The membrane proximal cytokine receptor domain of the human interleukin-6 receptor is sufficient for ligand binding but not for gp130 association.

1998

Interleukin-6 (IL-6) belongs to the family of the "four-helix bundle" cytokines. The extracellular parts of their receptors consist of several Ig- and fibronectin type III-like domains. Characteristic of these receptors is a cytokine-binding module consisting of two such fibronectin domains defined by a set of four conserved cysteines and a tryptophan-serine-X-tryptophan-serine (WSXWS) sequence motif. On target cells, IL-6 binds to a specific IL-6 receptor (IL-6R), and the complex of IL-6.IL-6R associates with the signal transducing protein gp130. The IL-6R consists of three extracellular domains. The NH2-terminal Ig-like domain is not needed for ligand binding and signal initiation. Here w…

Protein FoldingProtein ConformationEnzyme-Linked Immunosorbent AssayPlasma protein bindingImmunoglobulin domainBiologyLigandsBiochemistryHAMP domainAntigens CDCytokine Receptor gp130HumansMolecular BiologyDNA PrimersMembrane GlycoproteinsBase SequenceInterleukin-6Cell BiologyHydrogen-Ion ConcentrationGlycoprotein 130Precipitin TestsReceptors Interleukin-6Recombinant ProteinsCell biologyKineticsBiochemistryMATH domainSignal transductionCytokine receptorBinding domainProtein BindingSignal TransductionThe Journal of biological chemistry
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