4wv8

Crystal structure of a recombinant Vatairea macrocarpa seed lectin complexed with lactose

spinqualitylabelsall models 4wv8, resolution 1.83Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wv8 is a 4 chain structure with sequence from Vatairea macrocarpa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.83Å Ligands: CA, GAL, GLC, MN, PRD_900008 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LECS_VATMA Lectin that binds galactose. Publication Abstract from PubMed Legume 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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