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[[Image:1nt0.gif|left|200px]]


{{Structure
==Crystal structure of the CUB1-EGF-CUB2 region of MASP2==
|PDB= 1nt0 |SIZE=350|CAPTION= <scene name='initialview01'>1nt0</scene>, resolution 2.70&Aring;
<StructureSection load='1nt0' size='340' side='right'caption='[[1nt0]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|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>
<table><tr><td colspan='2'>[[1nt0]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NT0 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AHB:BETA-HYDROXYASPARAGINE'>AHB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nt0 OCA], [https://pdbe.org/1nt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nt0 RCSB], [https://www.ebi.ac.uk/pdbsum/1nt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nt0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MASP2_RAT 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nt/1nt0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nt0 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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 MASP2'''
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<ref>PMID:12743029</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1nt0" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Mannan-binding lectin serine protease|Mannan-binding lectin serine protease]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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: Davies JM]]
[[Category: Davies, J M.]]
[[Category: Drickamer K]]
[[Category: Drickamer, K.]]
[[Category: Feinberg H]]
[[Category: Feinberg, H.]]
[[Category: Uitdehaag JCM]]
[[Category: Uitdehaag, J C.M.]]
[[Category: Wallis R]]
[[Category: Wallis, R.]]
[[Category: Weis WI]]
[[Category: Weis, W I.]]
[[Category: CA]]
[[Category: EDO]]
[[Category: NAG]]
[[Category: cub domain]]
[[Category: egf like domain.]]
[[Category: mannose-binding protein]]
[[Category: masp]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:17 2008''
Retrieved from "https://proteopedia.org/1nt0"