2ok5: Difference between revisions

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[[Image:2ok5.jpg|left|200px]]<br /><applet load="2ok5" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2ok5.jpg|left|200px]]
caption="2ok5, resolution 2.30&Aring;" />
 
'''Human Complement factor B'''<br />
{{Structure
|PDB= 2ok5 |SIZE=350|CAPTION= <scene name='initialview01'>2ok5</scene>, resolution 2.30&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]
|GENE= CFB, BF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''Human Complement factor B'''
 


==Overview==
==Overview==
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==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 <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].  
2OK5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OK5 OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17310251 17310251]
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:[http://www.ncbi.nlm.nih.gov/pubmed/17310251 17310251]
[[Category: Alternative-complement-pathway C3/C5 convertase]]
[[Category: Alternative-complement-pathway C3/C5 convertase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: von willebrand factor-a domain]]
[[Category: von willebrand factor-a domain]]


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Revision as of 19:00, 20 March 2008

File:2ok5.jpg


PDB ID 2ok5

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: and
Gene: CFB, BF (Homo sapiens)
Activity: Alternative-complement-pathway C3/C5 convertase, with EC number 3.4.21.47
Coordinates: save as pdb, mmCIF, xml



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.

DiseaseDisease

Known diseases associated with this structure: Macular degeneration, age-related, reduced risk of OMIM:[138470]

About this StructureAbout this Structure

2OK5 is a Single protein structure of sequence from Homo sapiens. 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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