2WFV
Crystal structure of DILP5 variant C4
Summary for 2WFV
| Entry DOI | 10.2210/pdb2wfv/pdb |
| Related | 2WFU |
| Descriptor | PROBABLE INSULIN-LIKE PEPTIDE 5 A CHAIN, PROBABLE INSULIN-LIKE PEPTIDE 5 B CHAIN (3 entities in total) |
| Functional Keywords | signaling protein, cleavage on pair of basic residues |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) More |
| Cellular location | Secreted (Potential): Q7KUD5 Q7KUD5 |
| Total number of polymer chains | 2 |
| Total formula weight | 5248.00 |
| Authors | Kulahin, N.,Schluckebier, G.,Sajid, W.,De Meyts, P. (deposition date: 2009-04-15, release date: 2010-05-26, Last modification date: 2024-10-16) |
| Primary citation | Sajid, W.,Kulahin, N.,Schluckebier, G.,Ribel, U.,Henderson, H.R.,Tatar, M.,Hansen, B.F.,Svendsen, A.M.,Kiselyov, V.V.,Norgaard, P.,Wahlund, P.,Brandt, J.,Kohanski, R.A.,Andersen, A.S.,De Meyts, P. Structural and Biological Properties of the Drosophila Insulin-Like Peptide 5 Show Evolutionary Conservation. J.Biol.Chem., 286:661-, 2011 Cited by PubMed Abstract: We report the crystal structure of two variants of Drosophila melanogaster insulin-like peptide 5 (DILP5) at a resolution of 1.85 Å. DILP5 shares the basic fold of the insulin peptide family (T conformation) but with a disordered B-chain C terminus. DILP5 dimerizes in the crystal and in solution. The dimer interface is not similar to that observed in vertebrates, i.e. through an anti-parallel β-sheet involving the B-chain C termini but, in contrast, is formed through an anti-parallel β-sheet involving the B-chain N termini. DILP5 binds to and activates the human insulin receptor and lowers blood glucose in rats. It also lowers trehalose levels in Drosophila. Reciprocally, human insulin binds to the Drosophila insulin receptor and induces negative cooperativity as in the human receptor. DILP5 also binds to insect insulin-binding proteins. These results show high evolutionary conservation of the insulin receptor binding properties despite divergent insulin dimerization mechanisms. PubMed: 20974844DOI: 10.1074/JBC.M110.156018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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