The<unk>  protein complexes are both dimeric in structure, and, in each complex, the two monomers are linked to one another by a single disulfide bond. In addition, both complexes are derived from the same family of related genes and proteins but differ in their subunit composition. Below is a list of the most common<unk>  and<unk>  complexes and their subunit composition: Class<unk> y Complex Dimer subunits 1 2<unk> <unk> s FSH secretion<unk>  A α βA<unk>  B α βB<unk>  stimulates FSH secretion<unk>  A βA βA<unk>  AB βA βB<unk>  B βB βB Schematic diagram of the 1D structures of<unk>  and<unk> . The black line between the monomers represents a disulfide bond. The alpha and beta subunits share approximately 25% sequence similarity, whereas the similarity between beta subunits is approximately 65%. In mammals, four beta subunits have been described, called<unk>  βA,<unk>  βB,<unk>  βC and<unk>  βE.<unk>  βA and βB are identical to the two beta subunits of<unk> . A fifth subunit,<unk>  βD, has been described in Xenopus laevis. Two<unk>  βA subunits give rise to<unk>  A, one βA, and one βB subunit gives rise to<unk>  AB, and so on. Various, but not all theoretically possible, heterodimers have been described. The subunits are linked by a single covalent disulfide bond. The βC subunit is able to form<unk>  heterodimers with βA or βB subunits but is unable to dimerize with<unk>  α.
Activin and inhibin
Estrone/progesterone/testosterone
Estradiol/progesterone
Estrone/progesterone
SUSPUP and SUSPPUP
Estradiol/estrone/estriol
UPMC Central Pa
IPP-SHR