2ok5: Difference between revisions
New page: left|200px<br /> <applet load="2ok5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ok5, resolution 2.30Å" /> '''Human Complement fa... |
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'''Human Complement factor B'''<br /> | '''Human Complement factor B'''<br /> | ||
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==Overview== | ==Overview== | ||
Factor B is the central protease of the complement system of immune, defense. Here, we present the crystal structure of human factor B at 2.3-A, resolution, which reveals how the five-domain proenzyme is kept securely, inactive. The canonical activation helix of the Von Willebrand factor A, (VWA) domain is displaced by a helix from the preceding domain linker. The, two helices conformationally link the scissile-activation peptide and the, metal ion-dependent adhesion site required for binding of the ligand C3b., The data suggest that C3b binding displaces the three N-terminal control, domains and reshuffles the two central helices. Reshuffling of the helices, releases the scissile bond for final proteolytic activation and generates, a new interface between the VWA domain and the serine protease domain., This allosteric mechanism is crucial for tight regulation of the, complement-amplification step in the immune response. | Factor B is the central protease of the complement system of immune, defense. Here, we present the crystal structure of human factor B at 2.3-A, resolution, which reveals how the five-domain proenzyme is kept securely, inactive. The canonical activation helix of the Von Willebrand factor A, (VWA) domain is displaced by a helix from the preceding domain linker. The, two helices conformationally link the scissile-activation peptide and the, metal ion-dependent adhesion site required for binding of the ligand C3b., The data suggest that C3b binding displaces the three N-terminal control, domains and reshuffles the two central helices. Reshuffling of the helices, releases the scissile bond for final proteolytic activation and generates, a new interface between the VWA domain and the serine protease domain., This allosteric mechanism is crucial for tight regulation of the, complement-amplification step in the immune response. | ||
==About this Structure== | ==About this Structure== | ||
2OK5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alternative-complement-pathway_C3/C5_convertase Alternative-complement-pathway C3/C5 convertase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.47 3.4.21.47] Full crystallographic information is available from [http:// | 2OK5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alternative-complement-pathway_C3/C5_convertase Alternative-complement-pathway C3/C5 convertase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.47 3.4.21.47] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OK5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: von willebrand factor-a domain]] | [[Category: von willebrand factor-a domain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:04:09 2008'' | ||
Revision as of 16:04, 23 January 2008
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Human Complement factor B
OverviewOverview
Factor B is the central protease of the complement system of immune, defense. Here, we present the crystal structure of human factor B at 2.3-A, resolution, which reveals how the five-domain proenzyme is kept securely, inactive. The canonical activation helix of the Von Willebrand factor A, (VWA) domain is displaced by a helix from the preceding domain linker. The, two helices conformationally link the scissile-activation peptide and the, metal ion-dependent adhesion site required for binding of the ligand C3b., The data suggest that C3b binding displaces the three N-terminal control, domains and reshuffles the two central helices. Reshuffling of the helices, releases the scissile bond for final proteolytic activation and generates, a new interface between the VWA domain and the serine protease domain., This allosteric mechanism is crucial for tight regulation of the, complement-amplification step in the immune response.
About this StructureAbout this Structure
2OK5 is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Alternative-complement-pathway C3/C5 convertase, with EC number 3.4.21.47 Full crystallographic information is available from OCA.
ReferenceReference
Factor B structure provides insights into activation of the central protease of the complement system., Milder FJ, Gomes L, Schouten A, Janssen BJ, Huizinga EG, Romijn RA, Hemrika W, Roos A, Daha MR, Gros P, Nat Struct Mol Biol. 2007 Mar;14(3):224-8. Epub 2007 Feb 25. PMID:17310251
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