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      Sequence and functional relationships between androgen-binding protein/sex hormone-binding globulin and its homologs protein S, Gas6, laminin, and agrin.


      Agrin, chemistry, physiology, Alternative Splicing, Amino Acid Sequence, Androgen-Binding Protein, genetics, Animals, Binding Sites, Cytoskeletal Proteins, metabolism, Dystroglycans, Heparan Sulfate Proteoglycans, Humans, Intercellular Signaling Peptides and Proteins, Laminin, Membrane Glycoproteins, Molecular Sequence Data, Protein S, Proteins, Receptor Protein-Tyrosine Kinases, Sequence Homology, Sex Hormone-Binding Globulin, Signal Transduction

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          Androgen-binding protein/sex hormone-binding globulin (ABP/SHBG) is an extracellular binding protein that regulates the bioavailability of sex steroids. ABP/SHBG is closely related to the globular (G) domain of vitamin K-dependent protein S family of proteins and more distantly related to the G domains of several extracellular matrix proteins. ABP/SHBG appears to have evolved from the fusion of two ancestral G domains. Expanding evidence suggests that ABP/SHBG has other functions that are mediated through membrane binding, including signal transduction; however, the types of binding proteins (receptors) have not been identified. Sequence comparisons of ABP/SHBG with G domains of its homologs protein S, Gas6, laminin, and agrin have identified regions of ABP/SHBG that may bind receptors related to homolog receptors. These membrane receptors include beta-integrins, alpha-dystroglycan, and receptor tyrosine kinases. The G domains of laminin and related proteins have clearly evolved from a common ancestor to interact with specific receptors and binding proteins. It remains to be determined if ABP/SHBG followed this evolutionary pathway.

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