5t7p

Crystal structure of Pisum arvense lectin (PAL) complexed with X-Man

spinqualitylabelsall models 5t7p, resolution 2.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5t7p is a 2 chain structure with sequence from Pisum sativum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.16Å Ligands: CA, MN, XMM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LEC_PEA D-mannose specific lectin. Publication Abstract from PubMed The Pisum arvense lectin (PAL), a legume protein belonging to the Vicieae tribe, is capable of specific recognition of mannose, glucose and its derivatives without altering its structure. In this work, the three-dimensional structure of PAL was determined by X-ray crystallography and studied in detail by a combination of molecular docking and molecular dynamics (MD). Crystals belonging to monoclinic space group P21 were grown by the vapor diffusion method at 293 K. The structure was solved at 2.16 A and was similar to that of other Vicieae lectins. The structure presented Rfactor and Rfree of 17.04% and 22.08%, respectively, with all acceptable geometric parameters. Molecular docking was performed to analyze interactions of the lectin with monosaccharides, disaccharides and high-mannose N-glycans. PAL demonstrated different affinities on carbohydrates, depending on bond orientation and glycosidic linkage present in ligands. Furthermore, the lectin interacted with representative N-glycans in a manner consistent with the biological effects described for Vicieae lectins. Carbohydrate-recognition domain (CRD) in-depth analysis was performed by MD, describing the behavior of CRD residues in complex with ligand, stability, flexibility of the protein over time, CRD volume and topology. This is a first report of its kind for a lectin of the Vicieae tribe. Crystal structure of Pisum arvense seed lectin (PAL) and characterization of its interaction with carbohydrates by molecular docking and dynamics.,Pinto-Junior VR, Santiago MQ, Nobre CB, Osterne VJS, Leal RB, Cajazeiras JB, Lossio CF, Rocha BAM, Martins MGQ, Nobre CAS, Silva MTL, Nascimento KS, Cavada BS Arch Biochem Biophys. 2017 Jul 25;630:27-37. doi: 10.1016/j.abb.2017.07.013. PMID:28754321 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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