3FRP
Crystal Structure of Cobra Venom Factor, a Co-factor for C3- and C5 convertase CVFBb
Summary for 3FRP
| Entry DOI | 10.2210/pdb3frp/pdb |
| Descriptor | Cobra venom factor alpha chain, Cobra venom factor gamma chain, Cobra venom factor beta chain, ... (5 entities in total) |
| Functional Keywords | cobra venom factor, naja naja kouthia, complement c3 and c5 convertase cvfbb, complement proteins, complement alternate pathway, complement pathway, glycoprotein, immune response, inflammatory response, innate immunity, secreted, thioester bond, toxin, hydrolase cofactor |
| Biological source | Naja kaouthia (Monocled cobra) More |
| Cellular location | Secreted: Q91132 Q91132 Q91132 |
| Total number of polymer chains | 3 |
| Total formula weight | 141667.18 |
| Authors | Krishnan, V.,Narayana, S.V.L. (deposition date: 2009-01-08, release date: 2009-04-28, Last modification date: 2024-11-20) |
| Primary citation | Krishnan, V.,Ponnuraj, K.,Xu, Y.,Macon, K.,Volanakis, J.E.,Narayana, S.V. The Crystal Structure of Cobra Venom Factor, a Cofactor for C3- and C5-Convertase CVFBb. Structure, 17:611-619, 2009 Cited by PubMed 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. PubMed: 19368894DOI: 10.1016/j.str.2009.01.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.61 Å) |
Structure validation
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