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Molecular insights gained from covalently tethering cGMP to the ligand-binding sites of retinal rod cGMP-gated channels

Published online by Cambridge University Press:  04 February 2010

R. Lane Brown  and
Jeffrey W. Karpen
R. Lane Brown
Affiliation:
R. S. Dow Neurological Sciences Institute, Portland, OR 97209 and Department of Physiology, University of Colorado School of Medicine, Denver, CO 80262. karpenj@essex.hsc.colorado.edu
Jeffrey W. Karpen
Affiliation:
R. S. Dow Neurological Sciences Institute, Portland, OR 97209 and Department of Physiology, University of Colorado School of Medicine, Denver, CO 80262. karpenj@essex.hsc.colorado.edu
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Abstract

A photoaffinity analog of cGMP has been used to biochemically identify a new ligand-binding subunit of the retinal rod cGMP-activated ion channel, as well as amino acids in contact with cGMP in the original subunit. Covalent tethering of this probe to channels in excised menbrane patches has revealed a functional heteogeneity in the ligand-binding sites that may arise from the two biochemically identified subunits.

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Article Commentary
Information
Behavioral and Brain Sciences , Volume 18 , Special Issue 3: An International Journal of Current Research and Theory with Open Peer Commentary , September 1995 , pp. 471 - 472
Copyright
Copyright © Cambridge University Press 1995

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