1nt0

Crystal structure of the CUB1-EGF-CUB2 region of MASP2Crystal structure of the CUB1-EGF-CUB2 region of MASP2

Structural highlights 1nt0 is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , NonStd Res: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MASP2_RAT] Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase. 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 Serum mannose-binding proteins (MBPs) are C-type lectins that recognize cell surface carbohydrate structures on pathogens, and trigger killing of these targets by activating the complement pathway. MBPs circulate as a complex with MBP-associated serine proteases (MASPs), which become activated upon engagement of a target cell surface. The minimal functional unit for complement activation is a MASP homodimer bound to two MBP trimeric subunits. MASPs have a modular structure consisting of an N-terminal CUB domain, a Ca(2+)-binding EGF-like domain, a second CUB domain, two complement control protein modules and a C-terminal serine protease domain. The CUB1-EGF-CUB2 region mediates homodimerization and binding to MBP. The crystal structure of the MASP-2 CUB1-EGF-CUB2 dimer reveals an elongated structure with a prominent concave surface that is proposed to be the MBP-binding site. A model of the full six-domain structure and its interaction with MBPs suggests mechanisms by which binding to a target cell transmits conformational changes from MBP to MASP that allow activation of its protease activity. Crystal structure of the CUB1-EGF-CUB2 region of mannose-binding protein associated serine protease-2.,Feinberg H, Uitdehaag JC, Davies JM, Wallis R, Drickamer K, Weis WI EMBO J. 2003 May 15;22(10):2348-59. PMID:12743029 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Mannan-binding lectin serine protease

spinqualitylabelsall models 1nt0, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image