5UUY
Crystal structure of Dioclea lasiocarpa lectin (DLL) complexed with X-MAN
Summary for 5UUY
| Entry DOI | 10.2210/pdb5uuy/pdb |
| Descriptor | Dioclea lasiocarpa lectin (DLL), MANGANESE (II) ION, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | dioclea lasiocarpa, lectin, sugar binding protein |
| Biological source | Dioclea lasiocarpa |
| Total number of polymer chains | 1 |
| Total formula weight | 25935.73 |
| Authors | Santiago, M.Q.,Pinto-Junior, V.R.,Osterne, V.J.S.,Rocha, C.R.C.,Neco, A.H.B.,Fonseca, F.M.P.,Nascimento, K.S.,Cavada, B.S. (deposition date: 2017-02-17, release date: 2017-10-04, Last modification date: 2023-10-04) |
| Primary citation | Nascimento, K.S.,Santiago, M.Q.,Pinto-Junior, V.R.,Osterne, V.J.S.,Martins, F.W.V.,Nascimento, A.P.M.,Wolin, I.A.V.,Heinrich, I.A.,Martins, M.G.Q.,Silva, M.T.L.,Lossio, C.F.,Rocha, C.R.C.,Leal, R.B.,Cavada, B.S. Structural analysis of Dioclea lasiocarpa lectin: A C6 cells apoptosis-inducing protein. Int. J. Biochem. Cell Biol., 92:79-89, 2017 Cited by PubMed 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. PubMed: 28939357DOI: 10.1016/j.biocel.2017.09.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.88 Å) |
Structure validation
Download full validation report






