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Fluoroaluminates activate transducin‐GDP by mimicking the γ‐phosphate of GTP in its binding site
Author(s) -
Bigay Joëlle,
Deterre Philippe,
Pfister Claude,
Chabre Marc
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80004-1
Subject(s) - gtp' , transducin , chemistry , binding site , guanosine diphosphate , biochemistry , protein subunit , biophysics , stereochemistry , g protein , biology , enzyme , guanosine triphosphate , receptor , gene
Fluoride activation of the cGMP cascade of vision requires the presence of aluminum, and is shown to be mediated by the binding of one AlF‐ 4 to the GDP/GTP‐binding subunit of transducin. The presence of GDP in the site is required: AlF 4 − is ineffective when the site is empty or when GDPßS is substituted for GDP. This sensitivity to the sulfur of GDPßS suggests that AlF 4 − is in contact with the GDP. Striking structural similarities between AlF 4 − and PO 4 −1 lead us to propose that AlF 4 − mimics the role of the γ‐phosphate of GTP.