3kme | pdb_00003kme

Crystal structure of catalytic domain of TACE with phenyl-pyrrolidinyl-tartrate inhibitor

spinqualitylabelsall models 3kme, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kme is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: INN, IPA, Z59, ZN Related: 3kmc, 1bkc, 3ewj, 2fv9 Gene: ADAM17, CSVP, TACE (HUMAN) Activity: ADAM 17 endopeptidase, with EC number 3.4.24.86 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [ADA17_HUMAN] Defects in ADAM17 are a cause of neonatal inflammatory skin and bowel disease (NISBD) [MIM:614328]. NISBD is a disorder characterized by inflammatory features with neonatal onset, involving the skin, hair, and gut. The skin lesions involve perioral and perianal erythema, psoriasiform erythroderma, with flares of erythema, scaling, and widespread pustules. Gastrointestinal symptoms include malabsorptive diarrhea that is exacerbated by intercurrent gastrointestinal infections. The hair is short or broken, and the eyelashes and eyebrows are wiry and disorganized. Function [ADA17_HUMAN] Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Also involved in the activation of Notch pathway (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed A novel series of TNF-alpha convertase (TACE) inhibitors which are non-hydroxamate have been discovered. These compounds are bis-amides of L-tartaric acid (tartrate) and coordinate to the active site zinc in a tridentate manner. They are selective for TACE over other MMP's. We report the first X-ray crystal structure for a tartrate-based TACE inhibitor. The discovery of novel tartrate-based TNF-alpha converting enzyme (TACE) inhibitors.,Rosner KE, Guo Z, Orth P, Shipps GW Jr, Belanger DB, Chan TY, Curran PJ, Dai C, Deng Y, Girijavallabhan VM, Hong L, Lavey BJ, Lee JF, Li D, Liu Z, Popovici-Muller J, Ting PC, Vaccaro H, Wang L, Wang T, Yu W, Zhou G, Niu X, Sun J, Kozlowski JA, Lundell DJ, Madison V, McKittrick B, Piwinski JJ, Shih NY, Arshad Siddiqui M, Strickland CO Bioorg Med Chem Lett. 2010 Feb 1;20(3):1189-93. Epub 2009 Dec 5. PMID:20022498 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also A Disintegrin And Metalloproteinase 3D structures

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