1e5p
From Proteopedia
Crystal structure of aphrodisin, a sex pheromone from female hamster
Structural highlights
FunctionAPHR_CRICR Acts as an aphrodisiac pheromone, reliably eliciting copulatory behavior from male hamster. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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. Crystal structure of aphrodisin, a sex pheromone from female hamster.,Vincent F, Lobel D, Brown K, Spinelli S, Grote P, Breer H, Cambillau C, Tegoni M J Mol Biol. 2001 Jan 19;305(3):459-69. PMID:11152604[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
