1E5P
Crystal structure of aphrodisin, a sex pheromone from female hamster
Summary for 1E5P
Entry DOI | 10.2210/pdb1e5p/pdb |
Descriptor | APHRODISIN (2 entities in total) |
Functional Keywords | lipocalin, pheromone, hamster |
Biological source | MESOCRICETUS AURATUS (GOLDEN HAMSTER) |
Total number of polymer chains | 4 |
Total formula weight | 69556.45 |
Authors | Vincent, F.,Brown, K.,Spinelli, S.,Cambillau, C.,Tegoni, M. (deposition date: 2000-07-28, release date: 2001-07-26, Last modification date: 2024-10-16) |
Primary citation | Vincent, F.,Lobel, D.,Brown, K.,Spinelli, S.,Grote, P.,Breer, H.,Cambillau, C.,Tegoni, M. Crystal structure of aphrodisin, a sex pheromone from female hamster. J.Mol.Biol., 305:459-469, 2001 Cited by PubMed Abstract: We have solved the crystal structure of aphrodisin, a pheromonal protein inducing a copulatory behaviour in male hamster, using MAD methods with selenium, at 1.63 A resolution. The monomeric protein belongs to the lipocalin family, and possesses a disulfide bridge in a loop between strands 2 and 3. This disulfide bridge is characteristic of a family of lipocalins mainly identified in rodents, and is analogous to the fifth disulfide bridge of the long neurotoxins, such as alpha cobratoxin. An elongated electron density was found inside the buried cavity, which might represent a serendipitous ligand of unknown origin. The analysis of the water accessible surfaces of the side-chains bordering the cavity indicates that Phe76 may be the door for the natural ligand to access the cavity. This residue defines the entry of the cavity as belonging to the consensus for lipocalins. The face bearing Phe76 might also serve for the interaction with the receptor. PubMed: 11152604DOI: 10.1006/jmbi.2000.4241 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
Download full validation report
