5u38

Crystal structure of native lectin from Platypodium elegans seeds (PELa) complexed with Man1-3Man-OMe.

spinqualitylabelsall models 5u38, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5u38 is a 1 chain structure with sequence from Platypodium elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: CA, MAN, MMA, MN, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G1EUI6_9FABA Publication Abstract from PubMed A native lectin (nPELa), purified from seeds of the species Platypodium elegans, Dalbergieae tribe, was crystallized and structurally characterized by X-ray diffraction crystallography and bioinformatics tools. The obtained crystals diffracted to 1.6A resolution, and nPELa structure were solved through molecular substitution. In addition, nPELa has a metal binding site and a conserved carbohydrate recognition domain (CRD) similar to other Dalbergieae tribe lectins, such as PAL (Pterocarpus angolensis) and CTL (Centrolobium tomentosum). Molecular docking analysis indicated high affinity of this lectin for different mannosides, mainly trimannosides, formed by alpha-1,3 or alpha-1,6 glycosidic bond, as evidenced by the obtained scores. In addition, molecular dynamics simulations were performed to demonstrate the structural behavior of nPELa in aqueous solution. In solution, nPELa was highly stable, and structural modifications in its carbohydrate recognition site allowed interaction between the lectin and the different ligands. Different modifications were observed during simulations for each one of the glycans, which included different hydrogen bonds and hydrophobic interactions through changes in the relevant residues. In addition, nPELa was evaluated for its nociceptive activity in mice and was reported to be the first lectin of the Dalbergieae tribe to show CRD-dependent hypernociceptive activity. Structural studies and nociceptive activity of a native lectin from Platypodium elegans seeds (nPELa).,Cavada BS, Araripe DA, Silva IB, Pinto-Junior VR, Osterne VJS, Neco AHB, Laranjeira EPP, Lossio CF, Correia JLA, Pires AF, Assreuy AMS, Nascimento KS Int J Biol Macromol. 2017 Sep 1. pii: S0141-8130(17)32782-4. doi:, 10.1016/j.ijbiomac.2017.08.174. PMID:28867234 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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