The C1 homodimer of adenylyl cyclase binds nucleotides with high affinity but possesses exceedingly low catalytic activity

Neuroscience Letters

Volumn 467, Issue 1, 2009, Pages 1-5

  Suryanarayana, Srividya ^a   Pinto, Cibele ^a   Mou, Tung Chung ^b   Richter, Mark ^a   Lushington, Gerald H ^a   Seifert, Roland ^c  

^a UNIVERSITY OF KANSAS   (United States)

^b UNIVERSITY OF MONTANA   (United States)

^c HANNOVER MEDICAL SCHOOL   (Germany)

Author keywords

Adenylyl cyclase; Catalytic subunits; Dimerization; Fluorescence spectroscopy; Fluorescent nucleotides; Forskolin

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENYLATE CYCLASE; ADENYLATE CYCLASE INHIBITOR; ARGININE; GUANOSINE TRIPHOSPHATE; HISTIDINE; HOMODIMER; NUCLEOTIDE;

ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; DIMERIZATION; ENZYME ACTIVITY; FLUORESCENCE ANALYSIS; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; HUMAN CELL; MOLECULAR MECHANICS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; SIGNAL NOISE RATIO;

ADENOSINE TRIPHOSPHATE; ADENYLATE CYCLASE; ARGININE; ENZYME INHIBITORS; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; GUANOSINE TRIPHOSPHATE; HISTIDINE; MANGANESE; MODELS, CHEMICAL; MODELS, MOLECULAR; NUCLEOTIDES; PROTEIN MULTIMERIZATION;

EID: 70350324355     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neulet.2009.09.049     Document Type: Article

References (26)

1. Clark M., Cramer R.D.I., and van Opdenbosch N. Validation of the general purpose Tripos 5.2 force field. J. Comput. Chem. 10 (1989) 982-1012
2. Cooper D.M., and Crossthwaite A.J. Higher-order organization and regulation of adenylyl cyclases. Trends Pharmacol. Sci. 27 (2006) 426-431
3. Dessauer C.W., Scully T.T., and Gilman A.G. Interactions of forskolin and ATP with cytosolic domains of mammalian adenylyl cyclase. J. Biol. Chem. 272 (1997) 22272-22277
4. Gasteiger J., and Marsili M. Iterative partial equalization of orbital electronegativity: a rapid access to atomic charges. Tetrahedron 36 (1980) 3219-3228
5. Gille A., Lushington G.H., Mou T.C., Doughty M.B., Johnson R.A., and Seifert R. Differential inhibition of adenylyl cyclase isoforms and soluble guanylyl cyclase by purine and pyrimidine nucleotides. J. Biol. Chem. 279 (2004) 19955-19969
6. Göttle M., Dove S., Steindel P., Shen Y., Tang W.J., Geduhn J., König B., and Seifert R. Molecular analysis of the interaction of Bordetella pertussis adenylyl cyclase with fluorescent nucleotides. Mol. Pharmacol. 72 (2007) 526-535
7. Gu C., Cali J.J., and Cooper D.M. Dimerization of mammalian adenylate cyclases. Eur. J. Biochem. 269 (2002) 413-421
8. Hanoune J., and Defer N. Regulation and role of adenylyl cyclase isoforms. Annu. Rev. Pharmacol. Toxicol. 41 (2001) 145-174
9. Henikoff S., and Henikoff J.G. Performance evaluation of amino acid substitution matrices. Proteins 17 (1993) 49-61
10. Marti-Renom M.A., Stuart A.C., Fiser A., Sanchez R., Melo F., and Sali A. Comparative protein structure modeling of genes and genomes. Annu. Rev. Biophys. Biomol. Struct. 29 (2000) 291-325
11. 2+) binding site. Biochemistry 37 (1998) 16183-16191
12. Mou T.C., Gille A., Fancy D.A., Seifert R., and Sprang S.R. Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2′(3′)-O-(N-methylanthraniloyl)-guanosine 5′-triphosphate. J. Biol. Chem. 280 (2005) 7253-7261
13. Mou T.C., Gille A., Suryanarayana S., Richter M., Seifert R., and Sprang S.R. Broad specificity of mammalian adenylyl cyclase for interaction with 2′,3′-substituted purine- and pyrimidine nucleotide inhibitors. Mol. Pharmacol. 70 (2006) 878-886
14. Patel T.B., Du Z., Pierre S., Cartin L., and Scholich K. Molecular biological approaches to unravel adenylyl cyclase signaling and function. Gene 269 (2001) 13-25
15. Pinto C., Hübner M., Gille A., Richter M., Mou T.C., Sprang S.R., and Seifert R. Differential interactions of the catalytic subunits of adenylyl cyclase with forskolin analogs. Biochem Pharmacol 78 (2009) 62-69
16. Pinto C., Papa D., Hübner M., Mou T.C., Lushington G.H., and Seifert R. Activation and inhibition of adenylyl cyclase isoforms by forskolin analogs. J. Pharmacol. Exp. Ther. 325 (2008) 27-36
17. Sadana R., and Dessauer C.W. Physiological roles for G protein-regulated adenylyl cyclase isoforms: insights from knockout and overexpression studies. Neurosignals 17 (2009) 5-22
18. sα with the cytosolic domains of adenylyl cyclase. J. Biol. Chem. 272 (1997) 22265-22271
19. Sunahara R.K., and Taussig R. Isoforms of mammalian adenylyl cyclase: multiplicities of signalling. Mol. Interv. 2 (2002) 168-184
20. Suryanarayana S., Göttle M., Hübner M., Gille A., Mou T.C., Sprang S.R., Richter M., and Seifert R. Differential inhibition of various adenylyl cyclase isoforms and soluble guanylyl cyclase by 2′,3′-O-(2,4,6-trinitrophenyl)-substituted nucleoside 5′-triphosphates. J. Pharmacol. Exp. Ther. 330 (2009) 687-695
21. sα-GTPγS. Science 278 (1997) 1907-1916
22. Tesmer J.J., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., and Sprang S.R. Two-metal-ion catalysis in adenylyl cyclase. Science 285 (1999) 756-760
23. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
24. Wang J.L., Guo J.-X., Zhang Q.-Y., Wu J.J.-Q., Seifert R., and Lushington G.H. A conformational transition in the adenylyl cyclase catalytic site yields different binding modes for ribosyl-modified and unmodified nucleotide inhibitors. Bioorg. Med. Chem. 15 (2007) 2993-3002
25. 2+ regulation of adenylyl cyclases in cAMP microdomains. Physiol. Rev. 87 (2007) 965-1010
26. Zhang G., Liu Y., Ruoho A.E., and Hurley J.H. Structure of the adenylyl cyclase core. Nature 386 (1997) 247-253