7XKC
Crystal structure of Daucus Carrot hypoglycemic peptide (DCHP)
Summary for 7XKC
| Entry DOI | 10.2210/pdb7xkc/pdb |
| Descriptor | DCHP, SULFATE ION (3 entities in total) |
| Functional Keywords | daucus carrot, hypoglycemic peptide, a-glycosidase inhibitor., plant protein |
| Biological source | Daucus carota subsp. sativus |
| Total number of polymer chains | 4 |
| Total formula weight | 40965.99 |
| Authors | |
| Primary citation | Hao, Y.,Guo, T.,Ren, J.,Wang, Y.,Wang, L.,Shi, Y.,Feng, W. Characterization of a thermostable, protease-tolerant inhibitor of alpha-glycosidase from carrot: A potential oral additive for treatment of diabetes. Int.J.Biol.Macromol., 209:1271-1279, 2022 Cited by PubMed Abstract: Inhibiting α-glucosidase activity is important in controlling postprandial hyperglycemia and, thus, helping to manage type-2 diabetes mellitus (T2DM). In the present study, we purified a hypothetical protein of carrots called DCHP (Daucus Carrot hypoglycemic peptide), and their inhibitory effects on α-glucosidase, as well as related mechanisms, were investigated. The recombinant DCHP protein with a molecular weight of 8 kDa showed strong inhibitory activity against α-glycosidase and maintained good stability in solution. DCHP exhibited no inhibitory activity but was tolerant to trypsin and chymotrypsin. Cellular experiments demonstrated that glucose consumption and lactic acid production increased rapidly when treated with DCHP in Caco-2 and HepG2 cells. DCHP crystal was generated, and the crystal structure, which was similar to that of rBTI and consisted of a central α-helix and a two-stranded β-sheet with a unique loop region. The interaction between DCHP and α-glycosidase was investigated by molecular docking and site-directed mutation, which revealed that Glu43, Pro46, Thr47 Thr48 and Gln49 are the key residues in DCHP that inhibit α-glycosidase activity. This work provides potential bioactive peptides as functional foods or nutraceutical supplements in preventing and managing T2DM. PubMed: 35460754DOI: 10.1016/j.ijbiomac.2022.04.110 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.56 Å) |
Structure validation
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