Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant. mutation in ConA-like lectins

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorDelatorre, P.
dc.creatorRocha, BAM
dc.creatorGadelha, CAA
dc.creatorSanti-Gadelha, T.
dc.creatorCajazeiras, J. B.
dc.creatorSouza, E. P.
dc.creatorNascimento, K. S.
dc.creatorFreire, V. N.
dc.creatorSampaio, A. H.
dc.creatorAzevedo, W. F.
dc.creatorCavada, B. S.
dc.date2014-05-20T15:23:12Z
dc.date2016-10-25T17:57:04Z
dc.date2014-05-20T15:23:12Z
dc.date2016-10-25T17:57:04Z
dc.date2006-06-01
dc.date.accessioned2017-04-05T23:40:43Z
dc.date.available2017-04-05T23:40:43Z
dc.identifierJournal of Structural Biology. San Diego: Academic Press Inc. Elsevier B.V., v. 154, n. 3, p. 280-286, 2006.
dc.identifier1047-8477
dc.identifierhttp://hdl.handle.net/11449/34031
dc.identifierhttp://acervodigital.unesp.br/handle/11449/34031
dc.identifier10.1016/j.jsb.2006.03.011
dc.identifierWOS:000238104900007
dc.identifierhttp://dx.doi.org/10.1016/j.jsb.2006.03.011
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/878026
dc.descriptionThe crystal structure of Canavalia maritima lectin (ConM) complexed with trehalose and maltose revealed relevant point mutations in ConA-like lectins. ConM with the disaccharides and other ConA-like lectins complexed with carbohydrates demonstrated significant differences in the position of H-bonds. The main difference in the ConM structure is the replacement of Pro202 by Ser202, a residue that promotes the approximation of Tyr12 to the carbohydrate-binding site. The O-6' of the second glucose ring in maltose interacts with Tyr12, while in trehalose the interaction is established by the O-2' and Tyr12, explaining the higher affinity of ConM for disaccharides compared to monosaccharides. (c) 2006 Elsevier B.V. All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationJournal of Structural Biology
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectlectins
dc.subjectCanavalia maritima
dc.subjectCrystal structure
dc.subjectmutation
dc.titleCrystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant. mutation in ConA-like lectins
dc.typeOtro


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