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Crystal structure of a recombinant Vatairea macrocarpa seed lectin complexed with lactoseCrystal structure of a recombinant Vatairea macrocarpa seed lectin complexed with lactose
Structural highlights
FunctionLECS_VATMA Lectin that binds galactose. Publication Abstract from PubMedLegume lectins are the most thoroughly studied group of lectins and have been widely linked to many pathological processes. Their use as immunohistochemistry markers for cell profiling and cancer diagnosis have made these molecules important tools for immunological studies and have stimulated the prospection and characterization of new lectins. The crystal structures of a recombinant seed lectin from Vatairea macrocarpa (rVML) and its complexes with GalNAcalpha1-O-Ser, GalNAc and alpha-lactose, have been determined at 1.90, 1.97, 2.70 and 1.83A resolution, respectively. Small angle X-ray scattering and calorimetry assays have confirmed the same pH stable oligomerization pattern and binding profiles proposed for its wild-type counterpart. In silico analyzes have explored the potential of this recombinant lectin as new tool for cancer research through a comparative profile with other legume lectins widely used for cancer diagnosis and prognosis. The results suggest the recognition of specific epitopes exhibited on different cancer cells as a process that relies on the disposition of hydrophobic clusters and charged regions around the lectin carbohydrate-binding site, favouring the anchorage of different groups in the antigen boundaries, highlighting the different potential of each analyzed lectin. In conclusion, the experimental results and comparative analysis show that rVML is as a promising tool for cancer research, able to bind with high affinity specific tumor-associated antigens, highly stable and easily produced. Structural characterization of a Vatairea macrocarpa lectin in complex with a tumor-associated antigen: A new tool for cancer research.,Sousa BL, Silva-Filho JC, Kumar P, Graewert MA, Pereira RI, Cunha RM, Nascimento KS, Bezerra GA, Delatorre P, Djinovic-Carugo K, Nagano CS, Gruber K, Cavada BS Int J Biochem Cell Biol. 2016 Jan 2;72:27-39. doi: 10.1016/j.biocel.2015.12.016. PMID:26751394[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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