1nt0: Difference between revisions
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{{STRUCTURE_1nt0| PDB=1nt0 | SCENE= }} | |||
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'''Crystal structure of the CUB1-EGF-CUB2 region of MASP2''' | '''Crystal structure of the CUB1-EGF-CUB2 region of MASP2''' | ||
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[[Category: Wallis, R.]] | [[Category: Wallis, R.]] | ||
[[Category: Weis, W I.]] | [[Category: Weis, W I.]] | ||
[[Category: | [[Category: Cub domain]] | ||
[[Category: | [[Category: Egf like domain.]] | ||
[[Category: | [[Category: Mannose-binding protein]] | ||
[[Category: | [[Category: Masp]] | ||
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Revision as of 02:56, 3 May 2008
Crystal structure of the CUB1-EGF-CUB2 region of MASP2
OverviewOverview
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.
About this StructureAbout this Structure
1NT0 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 02:56:35 2008