2LAQ
Solution structure of the Sex Peptide from Drosophila melanogaster
Summary for 2LAQ
| Entry DOI | 10.2210/pdb2laq/pdb |
| NMR Information | BMRB: 17533 |
| Descriptor | Accessory gland-specific peptide 70A (1 entity in total) |
| Functional Keywords | hydroxiproline rich, signaling protein |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Cellular location | Secreted: P05623 |
| Total number of polymer chains | 1 |
| Total formula weight | 4435.04 |
| Authors | Moehle, K.,Freund, A.,Robinson, J.A. (deposition date: 2011-03-17, release date: 2011-04-27, Last modification date: 2023-06-14) |
| Primary citation | Moehle, K.,Freund, A.,Kubli, E.,Robinson, J.A. NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster. Febs Lett., 585:1197-1202, 2011 Cited by PubMed Abstract: The insect sex peptide (SP) elicits a variety of biological responses upon transfer to the mated female. SP contains 36 amino acids, including a tryptophan-rich N-terminal region, a central region containing five hydroxyproline (Hyp) residues, and a C-terminal region enclosed by a disulfide bridge. The solution structure of SP, studied here using NMR spectroscopy, includes a motif WPWN that adopts a type I β-turn in the N-terminal Trp-rich region. This turn region is connected to the central Hyp-rich region, which adopts extended and/or PPII-like conformations. The C-terminal disulfide-bonded loop populates helical turns or nascent helical structure. Overall, the results reveal a rather flexible peptide that lacks a compact folded structure in solution. PubMed: 21439282DOI: 10.1016/j.febslet.2011.03.040 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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