2ok5
From Proteopedia
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|PDB= 2ok5 |SIZE=350|CAPTION= <scene name='initialview01'>2ok5</scene>, resolution 2.30Å | |PDB= 2ok5 |SIZE=350|CAPTION= <scene name='initialview01'>2ok5</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= CFB, BF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CFB, BF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2i6q|2I6Q]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ok5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ok5 OCA], [http://www.ebi.ac.uk/pdbsum/2ok5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ok5 RCSB]</span> | ||
}} | }} | ||
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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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Macular degeneration, age-related, reduced risk of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=138470 138470]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Roos, A.]] | [[Category: Roos, A.]] | ||
[[Category: Schouten, A.]] | [[Category: Schouten, A.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: NAG]] | ||
[[Category: ccp domain]] | [[Category: ccp domain]] | ||
[[Category: pro-enzyme]] | [[Category: pro-enzyme]] | ||
| - | [[Category: serine protease domain | + | [[Category: serine protease domain,von willebrand factor-a domain]] |
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:19:01 2008'' |
Revision as of 01:19, 31 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | CFB, BF (Homo sapiens) | ||||||
| Activity: | Alternative-complement-pathway C3/C5 convertase, with EC number 3.4.21.47 | ||||||
| Related: | 2I6Q
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Human Complement factor B
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.
About this Structure
2OK5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 04:19:01 2008
Categories: Alternative-complement-pathway C3/C5 convertase | Homo sapiens | Single protein | Daha, M R. | Gomes, L. | Gros, P. | Hemrika, W. | Huizinga, E G. | Janssen, B J.C. | Milder, F J. | Romijn, R A. | Roos, A. | Schouten, A. | Ccp domain | Pro-enzyme | Serine protease domain,von willebrand factor-a domain
