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8SZO

Canavalia villosa lectin in complex with alpha-methyl-mannoside

Summary for 8SZO
Entry DOI10.2210/pdb8szo/pdb
DescriptorCanavalia villosa lectin, MANGANESE (II) ION, CALCIUM ION, ... (6 entities in total)
Functional Keywordscarbohydrate binding protein, plant lectin, beta-sandwich, pro-inflammatory, sugar binding protein, plant protein
Biological sourceCanavalia villosa
Total number of polymer chains1
Total formula weight26066.75
Authors
Primary citationLossio, C.F.,Moreira, C.G.,Amorim, R.M.F.,Nobre, C.S.,Silva, M.T.L.,Neto, C.C.,Pinto-Junior, V.R.,Silva, I.B.,Campos, J.,Assreuy, A.M.S.,Cavada, B.S.,Nascimento, K.S.
Lectin from Canavalia villosa seeds: A glucose/mannose-specific protein and a new tool for inflammation studies.
Int J Biol Macromol, 105:272-280, 2017
Cited by
PubMed Abstract: With important carbohydrate binding properties, lectins are proteins able to decipher the glycocode, and as such, they can be used in bioassays involving cell-cell communication, protein targeting, inflammation, and hypernociception, among others. In this study, a new glucose/mannose-specific lectin from Canavalia villosa seeds (Cvill) was isolated by a single affinity chromatography step in a Sephadex G-50 column, with a purification yield of 19.35mg of lectin per gram of powdered seed. Analysis of intact protein by mass spectrometry showed the lectin is composed of three polypeptide chains, including a 25.6kDa α chain, 12.9KDa β, and 12.6 KDa γ fragments, similar to the profile of ConA-like glucose/mannose-specific lectins. Partial sequence of the protein was obtained by MS-MALDI TOF/TOF covering 41.7% of its primary structure. Cvill presented sugar specificity to d-glucose, α-methyl-d-mannoside, d-mannose, and glycoproteins fetuin and ovoalbumin. The lectin characterization showed that Cvill presents high stability within a broad range of pH and temperature, also showing average toxicity against Artemia nauplii. The proinflammatory effect of Cvill was observed by induction of paw edema and hypernociception in mice, with the participation of the carbohydrate binding site, showing its potential to be used as tool in inflammation studies.
PubMed: 28693997
DOI: 10.1016/j.ijbiomac.2017.07.038
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

226707

數據於2024-10-30公開中

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