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The crystal structure of cobra venom factor, a cofactor for C3- and C5-convertase CVFBb.
- Source :
-
Structure (London, England : 1993) [Structure] 2009 Apr 15; Vol. 17 (4), pp. 611-9. - Publication Year :
- 2009
-
Abstract
- Cobra venom factor (CVF) is a functional analog of human complement component C3b, the active fragment of C3. Similar to C3b, in human and mammalian serum, CVF binds factor B, which is then cleaved by factor D, giving rise to the CVFBb complex that targets the same scissile bond in C3 as the authentic complement convertases C4bC2a and C3bBb. Unlike the latter, CVFBb is a stable complex and an efficient C5 convertase. We solved the crystal structure of CVF, isolated from Naja naja kouthia venom, at 2.6 A resolution. The CVF crystal structure, an intermediate between C3b and C3c, lacks the TED domain and has the CUB domain in an identical position to that seen in C3b. The similarly positioned CUB and slightly displaced C345c domains of CVF could play a vital role in the formation of C3 convertases by providing important primary binding sites for factor B.
- Subjects :
- Animals
Binding Sites genetics
Complement C3 Convertase, Alternative Pathway genetics
Complement C3-C5 Convertases genetics
Complement C3b genetics
Crystallography, X-Ray
Elapid Venoms genetics
Elapid Venoms isolation & purification
Elapid Venoms metabolism
Models, Chemical
Models, Molecular
Protein Binding genetics
Protein Structure, Secondary
Protein Structure, Tertiary
Complement C3 Convertase, Alternative Pathway metabolism
Complement C3-C5 Convertases metabolism
Complement C3b metabolism
Elapid Venoms chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0969-2126
- Volume :
- 17
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Structure (London, England : 1993)
- Publication Type :
- Academic Journal
- Accession number :
- 19368894
- Full Text :
- https://doi.org/10.1016/j.str.2009.01.015