5cis: Difference between revisions
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<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=5cis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cis OCA], [http://pdbe.org/5cis PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cis RCSB], [http://www.ebi.ac.uk/pdbsum/5cis PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cis ProSAT]</span></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=5cis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cis OCA], [http://pdbe.org/5cis PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cis RCSB], [http://www.ebi.ac.uk/pdbsum/5cis PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cis ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5cis" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:55, 1 February 2017
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+
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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