4L8Q

Crystal structure of Canavalia grandiflora seed lectin complexed with X-Man.

Summary for 4L8Q

• Entry DOI: 10.2210/pdb4l8q/pdb
• Related: 2CWM 2D7F 3A0K 3JU9
• Descriptor: Canavalia grandiflora seed lectin, CALCIUM ION, MANGANESE (II) ION, ... (8 entities in total)
• Functional Keywords: jelly roll domain, lectin, carbohydrate/sugar binding, protein bodies, sugar binding protein, plant protein
• Biological source: Canavalia grandiflora
• Total number of polymer chains: 1
• Total formula weight: 26730.18

Authors

Barroso-Neto, I.L.,Rocha, B.A.M.,Simoes, R.C.,Bezerra, M.J.B.,Pereira-Junior, F.N.,Osterne, V.J.S.,Nascimento, K.S.,Nagano, C.S.,Delatorre, P.,Sampaio, A.H.,Cavada, B.S. (deposition date: 2013-06-17, release date: 2014-05-21, Last modification date: 2023-09-20)

Primary citation

Barroso-Neto, I.L.,Simoes, R.C.,Rocha, B.A.,Bezerra, M.J.,Pereira-Junior, F.N.,Silva Osterne, V.J.,Nascimento, K.S.,Nagano, C.S.,Delatorre, P.,Pereira, M.G.,Freitas Pires, A.,Sampaio, A.H.,Assreuy, A.M.,Cavada, B.S.
Vasorelaxant activity of Canavalia grandiflora seed lectin: A structural analysis.
Arch.Biochem.Biophys., 543:31-39, 2014

PubMed Abstract: Lectins are comprised of a large family of proteins capable of the specific and reversible recognition of carbohydrates. Legume lectins, the most studied plant lectins, show high structural similarity, but with modifications that imply a variation in the intensity of some biological activities. In this work, the primary and tertiary structures of Canavalia grandiflora (ConGF) were determined. ConGF, a lectin isolated from C. grandiflora seeds, is able to induce relaxant activity in rat aortic rings. The complete sequence of ConGF comprises 237 amino acids. This particular protein has primary sequence variations commonly found in lectins from Dioclea and Canavalia genera. The protein structure was solved at 2.3 Å resolution by X-ray crystallography. An X-Man molecule was modeled into the carbohydrate recognition domain. Still, ConGF (30 and 100 μg mL(-1)) elicited 25% of vasorelaxation (IC50=34.48 ± 5.07 μg mL(-1)) in endothelialized aortic rings. A nonselective inhibitor of nitric oxide blocked ConGF relaxant effect, showing mediation by nitric oxide. Key distances between ConGF carbohydrate recognition domain residues were determined in order to explain this effect, in turn revealing some structural aspects that could differentiate lectins from the Canavalia genera with respect to different efficacy in vasorelaxant effect.

PubMed: 24361256
DOI: 10.1016/j.abb.2013.12.006

Experimental method

X-RAY DIFFRACTION (2.3 Å)