1nt0: Difference between revisions
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'''Crystal structure of the CUB1-EGF-CUB2 region of MASP2''' | {{Structure | ||
|PDB= 1nt0 |SIZE=350|CAPTION= <scene name='initialview01'>1nt0</scene>, resolution 2.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of the CUB1-EGF-CUB2 region of MASP2''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NT0 is a [ | 1NT0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NT0 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12743029 12743029] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: masp]] | [[Category: masp]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:17 2008'' | ||
Revision as of 11:01, 20 March 2008
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| 1nt0, resolution 2.70Å | |||||||||||||
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| Ligands: | NAG, CA and EDO | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of the CUB1-EGF-CUB2 region of MASP2
Overview
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 Structure
1NT0 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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
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