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.contributorPUCRA
dc.date.accessioned2014-05-20T15:23:12Z
dc.date.available2014-05-20T15:23:12Z
dc.date.created2014-05-20T15:23:12Z
dc.date.issued2006-06-01
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.identifier10.1016/j.jsb.2006.03.011
dc.identifierWOS:000238104900007
dc.description.abstractThe 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.relation3.433
dc.relation3,948
dc.rightsAcesso restrito
dc.sourceWeb of Science
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.typeArtículos de revistas


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