5TG3

Crystal Structure of Dioclea reflexa seed lectin (DrfL) in complex with X-Man

5TG3 の概要

• エントリーDOI: 10.2210/pdb5tg3/pdb
• 分子名称: Dioclea reflexa lectin, CALCIUM ION, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: lectin, dioclea reflexa, drfl, x-man, sugar binding protein
• 由来する生物種: Dioclea reflexa
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 104359.74

構造登録者

Santiago, M.Q.,Correia, J.L.A.,Pinto-Junior, V.R.,Osterne, V.J.S.,Pereira, R.I.,Silva-Filho, J.C.,Lossio, C.F.,Rocha, B.A.M.,Delatorre, P.,Neco, A.H.B.,Araripe, D.A.,Nascimento, K.S.,Cavada, B.S. (登録日: 2016-09-27, 公開日: 2017-02-15, 最終更新日: 2023-10-04)

主引用文献

Pinto-Junior, V.R.,Osterne, V.J.,Santiago, M.Q.,Correia, J.L.,Pereira-Junior, F.N.,Leal, R.B.,Pereira, M.G.,Chicas, L.S.,Nagano, C.S.,Rocha, B.A.,Silva-Filho, J.C.,Ferreira, W.P.,Rocha, C.R.,Nascimento, K.S.,Assreuy, A.M.,Cavada, B.S.
Structural studies of a vasorelaxant lectin from Dioclea reflexa Hook seeds: Crystal structure, molecular docking and dynamics.
Int. J. Biol. Macromol., 98:12-23, 2017

PubMed Abstract: The three-dimensional structure of Dioclea reflexa seed lectin (DrfL) was studied in detail by a combination of X-ray crystallography, molecular docking and molecular dynamics. DrfL was purified by affinity chromatography using Sephadex G-50 matrix. Its primary structure was obtained by mass spectrometry, and crystals belonging to orthorhombic space group P222 were grown by the vapor diffusion method at 293K. The crystal structure was solved at 1.765Å and was very similar to that of other lectins from the same subtribe. The structure presented R and R of 21.69% and 24.89%, respectively, with no residues in nonallowed regions of Ramachandran plot. Similar to other Diocleinae lectins, DrfL was capable of relaxing aortic rings via NO induction, with CRD participation, albeit with low intensity (32%). In silico analysis results demonstrated that DrfL could strongly interact with complex N-glycans, components of blood vessel glycoconjugates. Despite the high similarity among Diocleinae lectins, it was also reported that each lectin has unique CRD properties that influence carbohydrate binding, resulting in different biological effects presented by these molecules.

PubMed: 28130130
DOI: 10.1016/j.ijbiomac.2017.01.092

実験手法

X-RAY DIFFRACTION (1.765 Å)