The crystal structures of two spermadhesins reveal the CUB domain fold.
Spermadhesins, 12,000-14,000 M(r) mammalian proteins, include lectins involved in sperm-egg binding and display a single CUB domain architecture. We report the crystal structures of porcine seminal plasma PSP-I/PSP-II, a heterodimer of two glycosylated spermadhesins, and bovine aSFP at 2.4 A and 1.9 A resolution respectively.
Romero
A
A
Romão
M J
MJ
Varela
P F
PF
Kölln
I
I
Dias
J M
JM
Carvalho
A L
AL
Sanz
L
L
Töpfer-Petersen
E
E
Calvete
J J
JJ
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D018360:Crystallography, X-Ray; D019281:Dimerization; D005260:Female; D006023:Glycoproteins / Q000737:chemistry*; D006031:Glycosylation; D046911:Macromolecular Substances; D008297:Male; D008322:Mammals; D008961:Models, Structural; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D012661:Semen / Q000737:chemistry; D029607:Seminal Vesicle Secretory Proteins; D016415:Sequence Alignment; D013084:Sperm-Ovum Interactions; D013552:Swine
D006023:Glycoproteins; D046911:Macromolecular Substances; D029607:Seminal Vesicle Secretory Proteins; C074521:seminal vesicle secretory protein II, porcine; C074520:seminal vesicle secretory protein 109, porcine