| Literature DB >> 28939357 |
Kyria Santiago Nascimento1, Mayara Queiroz Santiago1, Vanir Reis Pinto-Junior1, Vinicius Jose Silva Osterne1, Francisco William Viana Martins1, Ana Paula Machado Nascimento2, Ingrid Alessandra Victoria Wolin2, Isabella Aparecida Heinrich2, Maria Gleiciane Queiroz Martins1, Mayara Torquato Lima Silva1, Claudia Figueiredo Lossio1, Cíntia Renata Costa Rocha3, Rodrigo Bainy Leal4, Benildo Sousa Cavada5.
Abstract
Lectins are multidomain proteins that specifically recognize various carbohydrates. The structural characterization of these molecules is crucial in understanding their function and activity in systems and organisms. Most cancer cells exhibit changes in glycosylation patterns, and lectins may be able to recognize these changes. In this work, Dioclea lasiocarpa seed lectin (DLL) was structurally characterized. The lectin presented a high degree of similarity with other lectins isolated from legumes, presenting a jelly roll motif and a metal-binding site stabilizing the carbohydrate-recognition domain. DLL demonstrated differential interactions with carbohydrates, depending on type of glycosidic linkage present in ligands. As observed by the reduction of cell viability in C6 cells, DLL showed strong antiglioma activity by mechanisms involving activation of caspase 3.Entities:
Keywords: Crystal structure; DLL; Dioclea lasiocarpa lectin; Glioma; Molecular docking
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Year: 2017 PMID: 28939357 DOI: 10.1016/j.biocel.2017.09.014
Source DB: PubMed Journal: Int J Biochem Cell Biol ISSN: 1357-2725 Impact factor: 5.085