Structural highlights
Function
[VM1BI_BOTMO] Snake venom zinc metalloproteinase that cleaves the alpha chain of fibrinogen (FGA) first followed by the beta chain (FGB) and shows no effect on the gamma chain. Cleaves only the beta chain of fibrin, leaving the gamma-dimer untouched. Shows proteolytic activity towards azocasein. Causes defibrinogenation when intraperitoneally administered on mice.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Hemostatically active snake venom metalloproteinases (SVMPs) perturb the blood coagulation cascade at specific points and due to their potential application as thrombolytic agents, the fibrin(ogen)olytic non-hemorrhagic SVMPs have been employed as biochemical tools in coagulation research and diagnosis. Structural studies complemented by the design of metalloproteinase inhibitors have been instrumental in understanding their stereo specificity and action mechanism. We present here, details of the crystal structure of BmooMPalpha-I, a 22.6 kDa non-hemorrhagic P-I class SVMP isolated from Bothrops moojeni venom, determined at 1.76 A resolution. In this structure, the catalytic zinc ion displays an unusual octahedral coordination formed by the three canonical histidines (His(142), His(146) and His(152)) and additionally, by three solvent molecules. Comparative sequence and structural studies indicate that the motif comprising amino acid segments 153-164 and 167-176 adjacent to the methionine-turn is a salient feature that differentiates both non and hemorrhagic P-I class SVMPs and could directly be involved in the development of the hemorrhagic activity.
Structural studies of BmooMPalpha-I, a non-hemorrhagic metalloproteinase from Bothrops moojeni venom.,Akao PK, Tonoli CC, Navarro MS, Cintra AC, Neto JR, Arni RK, Murakami MT Toxicon. 2010 Feb-Mar;55(2-3):361-8. Epub 2009 Aug 23. PMID:19706302[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bernardes CP, Santos-Filho NA, Costa TR, Gomes MS, Torres FS, Costa J, Borges MH, Richardson M, dos Santos DM, de Castro Pimenta AM, Homsi-Brandeburgo MI, Soares AM, de Oliveira F. Isolation and structural characterization of a new fibrin(ogen)olytic metalloproteinase from Bothrops moojeni snake venom. Toxicon. 2008 Mar 15;51(4):574-84. doi: 10.1016/j.toxicon.2007.11.017. Epub 2007 , Nov 24. PMID:18187176 doi:http://dx.doi.org/10.1016/j.toxicon.2007.11.017
- ↑ Akao PK, Tonoli CC, Navarro MS, Cintra AC, Neto JR, Arni RK, Murakami MT. Structural studies of BmooMPalpha-I, a non-hemorrhagic metalloproteinase from Bothrops moojeni venom. Toxicon. 2010 Feb-Mar;55(2-3):361-8. Epub 2009 Aug 23. PMID:19706302 doi:10.1016/j.toxicon.2009.08.013
