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Fluoroaluminates Activate Transducin-GDP by Mimicking the Gamma-phosphate of GTP in Its Binding Site

Overview
Journal FEBS Lett
Specialty Biochemistry
Date 1985 Oct 28
PMID 3863758
Citations 92
Authors
J Bigay
P Deterre
C Pfister
M Chabre
Affiliations
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Abstract

Fluoride activation of the cGMP cascade of vision requires the presence of aluminum, and is shown to be mediated by the binding of one A1F-4 to the GDP/GTP-binding subunit of transducin. The presence of GDP in the site is required: A1F-4 is ineffective when the site is empty or when GDP beta S is substituted for GDP. This sensitivity to the sulfur of GDP beta S suggests that A1F-4 is in contact with the GDP. Striking structural similarities between A1F-4 and PO3-4 lead us to propose that A1F-4 mimics the role of the gamma-phosphate of GTP.

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