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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Chemical Compound Review: 

AG-B-22749     [(2R,3R,4R,5R)-2-(2-amino-6- oxo-3H-purin-9...

Synonyms: SureCN1477429, CHEBI:74948, AC1L9GJM, CTK7J7602, 1rgl, ...
 
 
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High impact information on guanosine-2'-monophosphate

  • The complex formed between the enzyme ribonuclease T1 (EC 3.1.27.3) and its specific inhibitor 2'-guanylic acid (2'-GMP) has been refined to R = 0.180 using x-ray diffraction data to 1.9-A resolution [1].
  • Compared to wild-type RNaseT1 in complex with 2'-guanylic acid (2'GMP) both mutant inhibitor complexes indicate that the replacement of Trp59 by Tyr leads to a 0.04-nm inward shift of the single alpha-helix and to significant differences in the active-site geometry, inhibitor conformation and inhibitor binding [2].
  • Form I crystals were produced by microdialysis against 53% (v/v) 2-methyl-2,4-pentanediol in 0.01 M sodium acetate, 0.05% 2'-guanylic acid (2'GMP) and 0.02% NaN3 (pH 6.2-7.2) [3].
 

Analytical, diagnostic and therapeutic context of guanosine-2'-monophosphate

References

  1. Three-dimensional structure of the ribonuclease T1 2'-GMP complex at 1.9-A resolution. Arni, R., Heinemann, U., Tokuoka, R., Saenger, W. J. Biol. Chem. (1988) [Pubmed]
  2. X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59-->Tyr in ribonuclease T1. Schubert, W.D., Schluckebier, G., Backmann, J., Granzin, J., Kisker, C., Choe, H.W., Hahn, U., Pfeil, W., Saenger, W. Eur. J. Biochem. (1994) [Pubmed]
  3. Crystallization of a complex between ribonuclease T1 and 2'-guanylic acid. Heinemann, U., Wernitz, M., Pähler, A., Saenger, W., Menke, G., Rüterjans, H. Eur. J. Biochem. (1980) [Pubmed]
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