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1q0p
From Proteopedia
(New page: 200px<br /> <applet load="1q0p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q0p, resolution 1.8Å" /> '''A domain of Factor B...) |
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| - | [[Image:1q0p.gif|left|200px]]<br /> | + | [[Image:1q0p.gif|left|200px]]<br /><applet load="1q0p" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1q0p, resolution 1.8Å" /> | caption="1q0p, resolution 1.8Å" /> | ||
'''A domain of Factor B'''<br /> | '''A domain of Factor B'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Complement factor B is a 90 kDa protein consisting of three domains: a | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Q0P 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 MN as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1Q0P 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=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1Q0P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bhattacharya, A | + | [[Category: Bhattacharya, A A.]] |
| - | [[Category: Liddington, R | + | [[Category: Liddington, R C.]] |
[[Category: MN]] | [[Category: MN]] | ||
[[Category: a domain]] | [[Category: a domain]] | ||
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[[Category: von willebrand factor]] | [[Category: von willebrand factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:37 2008'' |
Revision as of 12:34, 21 February 2008
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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 diseases 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 with as ligand. Active as Alternative-complement-pathway C3/C5 convertase, with EC number 3.4.21.47 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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