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1q0p
From Proteopedia
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|PDB= 1q0p |SIZE=350|CAPTION= <scene name='initialview01'>1q0p</scene>, resolution 1.8Å | |PDB= 1q0p |SIZE=350|CAPTION= <scene name='initialview01'>1q0p</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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= BF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= BF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q0p OCA], [http://www.ebi.ac.uk/pdbsum/1q0p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q0p RCSB]</span> | ||
}} | }} | ||
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==Disease== | ==Disease== | ||
| - | Known | + | Known disease 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: Bhattacharya, A A.]] | [[Category: Bhattacharya, A A.]] | ||
[[Category: Liddington, R C.]] | [[Category: Liddington, R C.]] | ||
| - | [[Category: MN]] | ||
[[Category: a domain]] | [[Category: a domain]] | ||
[[Category: factor b]] | [[Category: factor b]] | ||
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[[Category: von willebrand factor]] | [[Category: von willebrand factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:07:11 2008'' |
Revision as of 20:07, 30 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | BF (Homo sapiens) | ||||||
| Activity: | Alternative-complement-pathway C3/C5 convertase, with EC number 3.4.21.47 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A domain of Factor B
Contents |
Overview
Complement factor B is a 90 kDa protein consisting of three domains: a three-module complement control protein, a von Willebrand factor A domain, and a C-terminal serine protease (SP) domain that adopts a default inactive (zymogen) conformation. The interaction between factor B and pathogen-bound C3b is mediated by its A domain, triggering a conformational change in factor B that ultimately creates the "C3 convertase" of the alternative complement pathway. We report the crystal structure of the A domain from factor B and show that it contains an integrin-like MIDAS motif that adopts the "open" conformation typical of integrin-ligand complexes, with an acidic residue (provided by a fortuitous crystal contact) completing the coordination of the metal ion. Modeling studies indicate that the factor B A domain can also adopt the closed conformation, supporting the hypothesis that an "integrin-like switch" is conserved in complement proteins and perhaps in 60 other A domains found within the human proteome.
Disease
Known disease associated with this structure: Macular degeneration, age-related, reduced risk of OMIM:[138470]
About this Structure
1Q0P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the A domain from complement factor B reveals an integrin-like open conformation., Bhattacharya AA, Lupher ML Jr, Staunton DE, Liddington RC, Structure. 2004 Mar;12(3):371-8. PMID:15016353
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