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| {{STRUCTURE_1nt0| PDB=1nt0 | SCENE= }} | | {{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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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12743029}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12743029 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12743029}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Mannose-binding protein]] | | [[Category: Mannose-binding protein]] |
| [[Category: Masp]] | | [[Category: Masp]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:56:35 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:59:22 2008'' |
