Cyclic GMP contact points within the 63-kDa subunit and a 240-kDa associated protein of retinal rod cGMP-activated channels

Biochemistry
R L BrownJ W Karpen

Abstract

Ion channels from retinal rods and a variety of other cells are directly gated by cyclic nucleotides. The rod channel is known to contain a 63-kDa subunit, and there is molecular genetic evidence for the existence, in human retina, of a second subunit with a deduced molecular mass of about 100 kDa. When purified from bovine rods, the channel consists of the 63-kDa subunit and a 240-kDa associated protein that has been shown recently to contain a version of the cloned second subunit as part of a larger complex. We had previously shown that a photoaffinity analog of cGMP, 8-(p-azidophenacylthio)-[32P]cGMP, specifically labels both the 63- and 240-kDa proteins. Here the analog was used to identify cGMP-binding regions and amino acid contact points within these proteins. The specific labeling of the 63-kDa subunit was localized to a 66 amino acid fragment (Tyr-515-Met-580) that is contained entirely within a 110 amino acid region proposed to be the cGMP-binding site on the basis of homology with other cyclic nucleotide-binding proteins. Within this fragment, amino acid residues Val-524, Val-525, and Ala-526 were found to contain label. These residues are part of a larger hydrophobic cluster that appears to line the binding pocket. ...Continue Reading

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Citations

Aug 1, 1996·Current Opinion in Neurobiology·R S Molday
Nov 1, 1996·Trends in Cardiovascular Medicine·M BielF Hofmann
Oct 6, 2001·Progress in Retinal and Eye Research·I M Pepe
Oct 24, 1995·Proceedings of the National Academy of Sciences of the United States of America·S E Gordon, W N Zagotta
Jan 20, 1999·Proceedings of the National Academy of Sciences of the United States of America·R L BrownJ W Crabb
Jan 19, 2000·Proceedings of the National Academy of Sciences of the United States of America·Y HeJ W Karpen
May 12, 2004·Neuron·Jie Zheng, William N Zagotta

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