Structural highlights
Function
[SFP1_BOVIN] Could enhance the fertilizing capacity of bull spermatozoa upon interaction with heparin-like glycosaminoglycans present in the female genital tract. Exhibits both simulatory and inhibitory actions on the release of pituitary gonadotropins.
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 PubMed
Bovine seminal plasma PDC-109 binds to sperm surface choline lipids and promotes sperm capacitation by stimulating the efflux of cholesterol and phospholipids. The structure of PDC-109 with bound phosphorylcholine was solved using MAD data of a single platinum site. Its two globular (40 x 50 x 20 A(3)) Fn2 domains are linked and clustered by a short polypeptide. The choline binding sites lie at the same face of the molecule. Phosphorylcholine binds to the Fn2 domains through a cation-pi interaction between the quaternary ammonium group and a core tryptophan, plus hydrogen bonding between hydroxyls of exposed tyrosines and the phosphate group. The structure of the PDC-109-oPC complex provides a structural ground for the sperm membrane-coating mechanism underlying PDC-109-induced capacitation.
Sperm coating mechanism from the 1.8 A crystal structure of PDC-109-phosphorylcholine complex.,Wah DA, Fernandez-Tornero C, Sanz L, Romero A, Calvete JJ Structure. 2002 Apr;10(4):505-14. PMID:11937055[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wah DA, Fernandez-Tornero C, Sanz L, Romero A, Calvete JJ. Sperm coating mechanism from the 1.8 A crystal structure of PDC-109-phosphorylcholine complex. Structure. 2002 Apr;10(4):505-14. PMID:11937055
