Abstract:
:Mammalian cGMP- and cAMP-dependent protein kinase show considerable similarity in amino acid sequence, although they specifically bind different cyclic nucleotides. Results of cGMP analogue binding experiments, combined with modeling of the cGMP binding sites by analogy to the structure of the homologous catabolite gene activator protein, suggest that a threonine residue forms a hydrogen bond with the 2-NH2 of cGMP. This threonine is invariant in all cGMP binding domains, but the corresponding residue in 23 out of 24 cAMP binding sites of protein kinases is alanine, which cannot form the same hydrogen bond. This alanine/threonine difference has the potential for discriminating between cAMP and cGMP and may be important in the evolutionary divergence of cyclic nucleotide binding sites.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Weber IT,Shabb JB,Corbin JDdoi
10.1021/bi00440a059subject
Has Abstractpub_date
1989-07-11 00:00:00pages
6122-7issue
14eissn
0006-2960issn
1520-4995journal_volume
28pub_type
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