Possible steroid binding site common to adrenal cytochrome P-450scc and prostatic steroid binding protein.
By searching the entire PIR-protein-sequence data base, we have found that a dodecapeptide sequence in bovine adrenal cytochrome P-450scc is closely related to that in rat prostatic steroid binding protein. The two proteins belong to unrelated protein families, but both have steroids as substrates or ligands. Thus, the dodecapeptides may be important for substrate/ligand recognition in the individual proteins.
D000311:Adrenal Glands / Q000032:analysis*; D000595:Amino Acid Sequence; D000727:Androgen-Binding Protein / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002352:Carrier Proteins / Q000378:metabolism*; D002417:Cattle; D003545:Cysteine; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D010446:Peptide Fragments; D060789:Prostatein; D011817:Rabbits; D051381:Rats; D060765:Secretoglobins; D014598:Uteroglobin; D060788:Mammaglobin B
D000727:Androgen-Binding Protein; D002352:Carrier Proteins; D003545:Cysteine; D003577:Cytochrome P-450 Enzyme System; D010446:Peptide Fragments; D060789:Prostatein; D060765:Secretoglobins; D014598:Uteroglobin; C511484:Scgb1d2 protein, rat; C511483:Scgb1d4 protein, rat; C556468:Scgb2a1 protein, rat; D060788:Mammaglobin B