Summary for 6IP9
| Entry DOI | 10.2210/pdb6ip9/pdb |
| Descriptor | Alpha-lactalbumin, SULFATE ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | lanthanum, bovine alpha-lactalbumin, hamlet, bamlet, metal binding protein |
| Biological source | Bos taurus (Bovine) |
| Total number of polymer chains | 1 |
| Total formula weight | 14529.11 |
| Authors | Prakash, P.,Yarramala, S.D.,Rao, C.P.,Bhaumik, P. (deposition date: 2018-11-02, release date: 2019-02-20, Last modification date: 2024-11-06) |
| Primary citation | Yarramala, D.S.,Prakash, P.,Ranade, D.S.,Doshi, S.,Kulkarni, P.P.,Bhaumik, P.,Rao, C.P. Cytotoxicity of apo bovine alpha-lactalbumin complexed with La3+on cancer cells supported by its high resolution crystal structure. Sci Rep, 9:1780-1780, 2019 Cited by PubMed Abstract: Cancer remains one of the biggest threats to human society. There are massive demands for compounds to selectively kill cancerous cells. Earlier studies have shown that bovine α -lactalbumin made lethal to tumor cells (BAMLET) becomes cytotoxic against cancer cells in complex with oleic acid {Hoque, M. et. al., PLoSOne 8, e68390 (2013)}. In our study, we obtained bovine α-lactalbumin complexed with lanthanum ion (La-B-α-LA) and determined its high resolution crystal structure. The natural calcium binding site of bovine α-lactalbumin is replaced by lanthanum. The La complex formation by B-α-apo-LA was also supported by various biophysical methods. Interestingly, our complex, La-B-α-LA exhibits much greater anticancer activity against breast cancer cells as compared to the reported BAMLET-oleic acid complex. This study shows that La-B-α-LA complex is preferentially more toxic to MCF-7 cells as compared to KB (oral cancer) and HeLa (cervical) cells, while almost non-toxic to the healthy cells that we studied. Our data indicates that the cytotoxicity of La-B-α-LA against cancer cells is through apoptotic path way. The higher anticancer activity of La-B-α-LA is attributable to the requisite structural changes induced in the protein by La binding as supported by the crystal structure of the complex. PubMed: 30741951DOI: 10.1038/s41598-018-38024-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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