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The key to rhodopsin function lies in the structure of its interface with transducin

Published online by Cambridge University Press:  04 February 2010

Edward A. Dratz
Edward A. Dratz*
Affiliation:
Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717. uched@msu.oscs.montana.edu or dratz@chemistry.montana.edu
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Abstract

Light activated rhodopsin functions by catalyzing the exchange of GTP for GDP on numerous copies of transducin. Peptide mapping has shown that at least six regions, three on rhodopsin and three on the transducin alpha subunit, are involved in the active interface between the two proteins. The most informative structural studies of rhodopsin should include focus on the transducin interaction.

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Article Commentary
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Behavioral and Brain Sciences , Volume 18 , Special Issue 3: An International Journal of Current Research and Theory with Open Peer Commentary , September 1995 , pp. 473 - 474
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Copyright © Cambridge University Press 1995

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