5F5Q

Crystal structure of Canavalia virosa lectin in complex with alpha-methyl-mannoside

5F5Q の概要

• エントリーDOI: 10.2210/pdb5f5q/pdb
• 分子名称: Concanavalin-A, CALCIUM ION, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: metal binding protein, sugar binding protein
• 由来する生物種: Canavalia cathartica (Jackbean)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51586.86

構造登録者

Osterne, V.J.S.,Silva-Filho, J.C.,Pinto-Junior, V.R.,Santiago, M.Q.,Lossio, C.F.,Delatorre, P.,Nascimento, K.S.,Cavada, B.S. (登録日: 2015-12-04, 公開日: 2016-10-26, 最終更新日: 2023-09-27)

主引用文献

Osterne, V.J.,Silva-Filho, J.C.,Santiago, M.Q.,Pinto-Junior, V.R.,Almeida, A.C.,Barreto, A.A.,Wolin, I.A.,Nascimento, A.P.,Amorim, R.M.,Rocha, B.A.,Delatorre, P.,Nagano, C.S.,Leal, R.B.,Assreuy, A.M.,Nascimento, K.S.,Cavada, B.S.
Structural characterization of a lectin from Canavalia virosa seeds with inflammatory and cytotoxic activities.
Int.J.Biol.Macromol., 94:271-282, 2016

PubMed Abstract: A lectin from Canavalia virosa, Diocleinae subtribe, was purified by affinity chromatography with Sephadex G-50 matrix and named ConV. The primary structure of ConV was obtained by mass spectrometry and crystals were obtained by the vapor diffusion method at 293K and belonged to orthorhombic space group P222 with two molecules in its asymmetric unit. The structure obtained presented R and R of 18.91% and 24.92% respectively, with no residues in nonallowed regions of Ramachandran plot. The crystal structure was solved at 2.53Å and was demonstrated to be very similar to other lectins from the same subtribe. In inflammatory tests, ConV elicited paw edema, but incubation of lectin with glucose beforehand was able to reduce the edematogenic effect, indicating the involvement of the carbohydrate recognition domain in this process. The lectin also showed toxicity to rat C6 glioma cells, disrupting the mitochondrial membrane potential (ΔYm) and decreasing cell viability, indicating an anticancer potential for ConV. In silico studies confirmed that ConV interacts strongly with carbohydrates that comprise the N-glycans of glycoproteins. This finding corroborates the hypothesis which holds that the lectin domain interacts with glycans in molecular targets and that this contributes to the effects observed in biological activities.

PubMed: 27737777
DOI: 10.1016/j.ijbiomac.2016.10.020

実験手法

X-RAY DIFFRACTION (2.52 Å)