Structural highlights
Function
CONA_CANGL Glucose/D-mannose/rhamnose specific lectin. Has hemagglutinating activity towards rabbit erythrocytes. Has mitogenic activity towards murine splenocytes that is inhibited by glucose. Inhibits HIV-1 reverse transcriptase with an IC(50) of 35uM. Has a potent antiproliferative activity against L1210 leukemia cells in vitro that is not inhibited by glucose. Inhibits translation in cell-free rabbit reticulocyte system with an IC(50) of 2.08uM. Lacks anti-fungal activity against M.arachidicola, B.cenera and F.oxysporum.[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
Plant lectins, especially those purified from species of the Leguminosae family, represent the best studied group of carbohydrate-binding proteins. The legume lectins from Diocleinae subtribe are highly similar proteins that present significant differences in the potency/efficacy of their biological activities. The structural studies of the interactions between lectins and sugars may clarify the origin of the distinct biological activities observed in this high similar class of proteins. In this way, this work presents a crystallographic study of the ConM and CGL (agglutinins from Canavalia maritima and Canavalia gladiata, respectively) in the following complexes: ConM/CGL:Man(alpha1-2)Man(alpha1-O)Me, ConM/CGL:Man(alpha1-3)Man(alpha1-O)Me and ConM/CGL:Man(alpha1-4)Man(alpha1-O)Me, which crystallized in different conditions and space group from the native proteins. The structures were solved by molecular replacement, presenting satisfactory values for R(factor) and R(free). Comparisons between ConM, CGL and ConA (Canavalia ensiformis lectin) binding mode with the dimannosides in subject, presented different interactions patterns, which may account for a structural explanation of the distincts biological properties observed in the lectins of Diocleinae subtribe.
Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: new insights into the understanding of the structure-biological activity relationship in legume lectins.,Bezerra GA, Oliveira TM, Moreno FB, de Souza EP, da Rocha BA, Benevides RG, Delatorre P, de Azevedo WF Jr, Cavada BS J Struct Biol. 2007 Nov;160(2):168-76. Epub 2007 Aug 16. PMID:17881248[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wong JH, Ng TB. Isolation and characterization of a glucose/mannose/rhamnose-specific lectin from the knife bean Canavalia gladiata. Arch Biochem Biophys. 2005 Jul 1;439(1):91-8. PMID:15935326 doi:http://dx.doi.org/S0003-9861(05)00186-4
- ↑ Bezerra GA, Oliveira TM, Moreno FB, de Souza EP, da Rocha BA, Benevides RG, Delatorre P, de Azevedo WF Jr, Cavada BS. Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: new insights into the understanding of the structure-biological activity relationship in legume lectins. J Struct Biol. 2007 Nov;160(2):168-76. Epub 2007 Aug 16. PMID:17881248 doi:http://dx.doi.org/10.1016/j.jsb.2007.07.012
