Regular ArticleThe Crystal Structure of the Complexes of Concanavalin A with 4′-Nitrophenyl-α-d-mannopyranoside and 4′-Nitrophenyl-α-d-glucopyranoside
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One century of ConA and 40 years of ConBr research: A structural review
2019, International Journal of Biological MacromoleculesCitation Excerpt :A triclinic crystal was also observed in Concanavalin A (PDB id 1VLN) [49], along with dimerized ConA (PDB id 1GKB) [50]. In 1996, ConA complexed with ligands 4′-nitrophenyl-α-D-mannopyranoside (PDB id 1VAM) and 4′-nitrophenyl-α-D-glucopyranoside (PDB id 1VAL) was also deposited, allowing comparative studies between the lectin and both mannoside and glucoside interactions [51]. In 1999, Dimick and collaborators observed the ability of ConA to form aggregates with multivalent ligands by formation of crosslinks (PDB id 1QGL) [52].
Multivalent Carbohydrate-Functionalized Polymer Nanocrystals
2019, BiomacromoleculesStructural analysis of a Dioclea sclerocarpa lectin: Study on the vasorelaxant properties of Dioclea lectins
2016, International Journal of Biological MacromoleculesCitation Excerpt :The stabilization of the crystal structure in the presence of X-man has been previously described for other mannose-binding legume lectins, such as D. violacea [10], Canavalia grandiflora [19], Canavalia boliviana [40], and Camptosema pedicellatum [41]. Teixeira et al. demonstrated that the indole group from X-man in the structure of C. pedicellatum lectin is oriented in CRD by the Val99 residue which has contact with the hydrophobic indole, thus confirming the importance of hydrophobic contacts in the anchorage of carbohydrates in the CRD [42]. Phe induced tonic contractions in aortas with amplitude of 0.811 ± 0.35 g (n = 11) in the absence and 0.714 ± 0.149 g (n = 10) in the presence of endothelium.
Hepatic serum amyloid A1 aggravates T cell-mediated hepatitis by inducing chemokines via toll-like receptor 2 in mice
2015, Journal of Biological ChemistryInteractions between indole-3-acetic acid (IAA) with a lectin from Canavalia maritima seeds reveal a new function for lectins in plant physiology
2013, BiochimieCitation Excerpt :However, lectins from leguminous and other plant families, as well as other organisms [35], might also interact with other molecules, such as nonprotein amino acids [36] and hydrophobic compounds [29,37–39]. In the latter case, studies have been performed with the fluorescent probes ANS (8-anilinonaphthalene-1-sulfonate) and TNS (2-ρ-toluidinonaphthalene-6-sulfonate) [37,40], adenine [41–43], hydrophobic sugar derivatives [44,45] and the auxin IAA [29]. ConM is a lectin isolated from the seeds of the leguminous plant Canavalia maritima, which is commonly known as the bay bean, sand bean, beach bean or MacKenzie bean.
Immune mechanisms of Concanavalin a model of autoimmune hepatitis
2012, World Journal of Gastroenterology
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