The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Regulatory Subunit Of Protein Kinase A: Structure of Deletion Mutant with cAMP Binding Domains
Abstract
In the molecular scheme of living organisms, adenosine 3′,5′-monophosphate (cyclic AMP or cAMP) has been a universal second messenger. In eukaryotic cells, the primary receptors for cAMP are the regulatory subunits of cAMP-dependent protein kinase. The crystal structure of a 1-91 deletion mutant of the type Iα regulatory subunit was refined to 2.8 Å resolution. Each of the two tandem cAMP binding domains provides an extensive network of hydrogen bonds that buries the cyclic phosphate and the ribose between two β strands that are linked by a short α helix. Each adenine base stacks against an aromatic ring that lies outside the β barrel. This structure provides a molecular basis for understanding how cAMP binds cooperatively to its receptor protein, thus mediating activation of the kinase.
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Cites
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Cited by
Scott, J. W., Hawley, S. A., Green, K. A., Anis, M., Stewart, G., Scullion, G. A., Norman, D. G., & Hardie, D. G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19874 · Cited by 754
Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729
A novel Epac-specific cAMP analogue demonstrates independent regulation of Rap1 and ERK
Enserink, J. M., Christensen, A. E., de Rooij, J., van Triest, M., Schwede, F., Genieser, H. G., Døskeland, S. O., Blank, J. L., & Bos, J. L. (2002) · Nature Cell Biology · doi:10.1038/ncb874 · Cited by 625
Skalhegg, B. (2000) · Frontiers in Bioscience · doi:10.2741/skalhegg · Cited by 482
cAMP-GEFII is a direct target of cAMP in regulated exocytosis
Ozaki, N., Shibasaki, T., Kashima, Y., Miki, T., Takahashi, K., Ueno, H., Sunaga, Y., Yano, H., Matsuura, Y., Iwanaga, T., et al. (2000) · Nature Cell Biology · doi:10.1038/35041046 · Cited by 481
Metadata
- Authors
- Su, Y., Dostmann, W. R. G., Herberg, F. W., Durick, K., Xuong, N.-H., Ten Eyck, L., Taylor, S. S., & Varughese, K. I.
- Venue
- Science
- Published
- 1995-08-11
- Volume
- 269
- Issue
- 5225
- Pages
- 807-813
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2132023176
- Cited by
- 393
- References
- 1
- FWCI
- 5.68
- Type
- journal article
- Language
- en
- Open access
- closed
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- Su, Y., Dostmann, W. R. G., Herberg, F. W., Durick, K., Xuong, N.-H., Ten Eyck, L., Taylor, S. S., & Varughese, K. I. (1995). Regulatory Subunit Of Protein Kinase A: Structure of Deletion Mutant with cAMP Binding Domains. Science. https://doi.org/10.1126/science.7638597
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