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[[Image:1nt0.gif|left|200px]]<br /><applet load="1nt0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nt0, resolution 2.70&Aring;" />
'''Crystal structure of the CUB1-EGF-CUB2 region of MASP2'''<br />


==Overview==
==Crystal structure of the CUB1-EGF-CUB2 region of MASP2==
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.
<StructureSection load='1nt0' size='340' side='right'caption='[[1nt0]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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/initialview01.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>


==About this Structure==
==See Also==
1NT0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NT0 OCA].
*[[Mannan-binding lectin serine protease|Mannan-binding lectin serine protease]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12743029 12743029]
[[Category: Large Structures]]
[[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 Feb 21 14:09:38 2008''

Latest revision as of 11:52, 10 April 2024

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 Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:, , ,
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.

See Also

1nt0, resolution 2.70Å

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