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==The CUB1-EGF-CUB2 domains of rat MBL-associated serine protease-2 (MASP-2) bound to Ca2+==
==The CUB1-EGF-CUB2 domains of rat MBL-associated serine protease-2 (MASP-2) bound to Ca2+==
<StructureSection load='5ckn' size='340' side='right' caption='[[5ckn]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='5ckn' size='340' side='right'caption='[[5ckn]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ckn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CKN FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ckn]] 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=5CKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CKN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ckn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ckn OCA], [http://pdbe.org/5ckn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ckn RCSB], [http://www.ebi.ac.uk/pdbsum/5ckn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ckn ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5ckn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ckn OCA], [https://pdbe.org/5ckn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ckn RCSB], [https://www.ebi.ac.uk/pdbsum/5ckn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ckn ProSAT]</span></td></tr>
</table>
</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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The lectin pathway of complement is activated by complexes comprising a recognition component (mannose-binding lectin, serum ficolins, collectin-LK or collectin-K1) and a serine protease (MASP-1 or MASP-2). MASP-1 activates MASP-2, and MASP-2 cleaves C4 and C4b-bound C2. To clarify activation, new crystal structures of Ca2+-bound MASP dimers were determined, together with their solution structures from X-ray scattering, analytical ultracentrifugation, and atomistic modeling. Solution structures of the CUB1-EGF-CUB2 dimer of each MASP indicate that the two CUB2 domains were tilted by as much as 90 degrees compared with the crystal structures, indicating considerable flexibility at the EGF-CUB2 junction. Solution structures of the full-length MASP dimers in their zymogen and activated forms revealed similar structures that were much more bent than anticipated from crystal structures. We conclude that MASP-1 and MASP-2 are flexible at multiple sites and that this flexibility may permit both intra- and inter-complex activation.
Flexibility in Mannan-Binding Lectin-Associated Serine Proteases-1 and -2 Provides Insight on Lectin Pathway Activation.,Nan R, Furze CM, Wright DW, Gor J, Wallis R, Perkins SJ Structure. 2017 Jan 18. pii: S0969-2126(16)30404-X. doi:, 10.1016/j.str.2016.12.014. PMID:28111019<ref>PMID:28111019</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ckn" style="background-color:#fffaf0;"></div>
==See Also==
*[[Mannan-binding lectin serine protease|Mannan-binding lectin serine protease]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Furze, C M]]
[[Category: Large Structures]]
[[Category: Gor, J]]
[[Category: Rattus norvegicus]]
[[Category: Nan, R]]
[[Category: Furze CM]]
[[Category: Perkins, S J]]
[[Category: Gor J]]
[[Category: Wallis, R]]
[[Category: Nan R]]
[[Category: Wright, D W]]
[[Category: Perkins SJ]]
[[Category: Complement activation]]
[[Category: Wallis R]]
[[Category: Cub1-egf-cub2]]
[[Category: Wright DW]]
[[Category: Hydrolase]]
[[Category: Lectin pathway]]
[[Category: Masp]]

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