Assignment of backbone resonances in a eukaryotic protein kinase - ERK2 as a representative example

Methods in Molecular Biology

Volumn 831, Issue , 2012, Pages 359-368

  Piserchio, Andrea ^a   Dalby, Kevin N ^b   Ghose, Ranajeet ^a,c  

^a CITY COLLEGE OF NEW YORK   (United States)

^b UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^c CITY UNIVERSITY OF NEW YORK   (United States)

Author keywords

Backbone resonance assignment; ERK2; MAP kinase; Selective labeling; Spin labeled ATP; TROSY

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE 1;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; SPIN LABELING;

MITOGEN-ACTIVATED PROTEIN KINASE 1; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; SPIN LABELS;

EUKARYOTA;

EID: 84855882586     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-480-3_19     Document Type: Article

References (32)

1. Murphy, L. O., and Blenis, J. (2006) MAPK signal specificity: the right place at the right time. Trends Biochem. Sci. 31, 268-275. (Pubitemid 43674354)
2. Chen, Z., Gibson, T. B., Robinson, F., Silvestro, L., Pearson, G., Xu, B., Wright, A., Vanderbilt, C., and Cobb, M. H. (2001) MAP kinases. Chem. Rev. 101, 2449-2476. (Pubitemid 35373029)
3. Pearson, G., Robinson, F., Beers Gibson, T., Xu, B. E., Karandikar, M., Berman, K., and Cobb, M. H. (2001) Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocrine Rev. 22, 153-183. (Pubitemid 32458157)
4. Fang, J. Y., and Richardson, B. C. (2005) The MAPK signalling pathways and colorectal cancer. The Lancet Oncol. 6, 322-327. (Pubitemid 40590269)
5. Kohno, M., and Pouyssegur, J. (2006) Targeting the ERK signaling pathway in cancer therapy. Annal. Med. 38, 200-211. (Pubitemid 43675585)
6. Kohno, M., and Pouyssegur, J. (2003) Pharmacological inhibitors of the ERK signaling pathway: application as anticancer drugs. Prog. Cell Cyc. Res. 5, 219-224.
7. Roux, P. P., and Blenis, J. (2004) ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions. Microbiol. Mol. Biol. Rev. 68, 320-344. (Pubitemid 38756868)
8. Piserchio, A., Dalby, K. N., and Ghose, R. (2012) Expression and Purification of Srcfamily Kinases for Solution NMR Studies. Meth. Mol. Biol. 831, 111-132.
9. Sattler, M., Schleucher, J., and Griesinger, C. (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. NMR Spectr. 34, 93-158. (Pubitemid 129595216)
10. Salzmann, M., Pervushin, K., Wider, G., Senn, H., and Wuthrich, K. (1998) TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. Proc. Natl. Acad. Sci. USA 95, 13585-13590. (Pubitemid 28523015)
11. Masterson, L. R., Mascioni, A., Traaseth, N. J., Taylor, S. S., and Veglia, G. (2008) Allosteric cooperativity in protein kinase A. Proc. Natl. Acad. Sci. USA 105, 506-511. (Pubitemid 351171738)
12. Masterson, L. R., Cheng, C., Yu, T., Tonelli, M., Kornev, A., Taylor, S. S., and Veglia, G. (2010) Dynamics connect substrate recognition to catalysis in protein kinase A. Nature Chem. Biol. 6, 821-828.
13. Wiesner, S., Wybenga-Groot, L. E., Warner, N., Lin, H., Pawson, T., Forman-Kay, J. D., and Sicheri, F. (2006) A change in conformational dynamics underlies the activation of Eph receptor tyrosine kinases. EMBO J. 25, 4686-4696. (Pubitemid 44498140)
14. Vajpai, N., Strauss, A., Fendrich, G., Cowan-Jacob, S. W., Manley, P. W., Grzesiek, S., and Jahnke, W. (2008) Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib. J. Biol. Chem. 283, 18292-18302.
15. Vogtherr, M., Saxena, K., Hoelder, S., Grimme, S., Betz, M., Schieborr, U., Pescatore, B., Robin, M., Delarbre, L., Langer, T., Wendt, K. U., and Schwalbe, H. (2006) NMR characterization of kinase p38 dynamics in free and ligand-bound forms. Angew. Chem. Intl. Ed. Engl. 45, 993-997. (Pubitemid 43198494)
16. Riek, R., Pervushin, K., and Wuthrich, K. (2000) TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution. Trends Biochem. Sci. 25, 462-468.
17. Pervushin, K. (2000) Impact of transverse relaxation optimized spectroscopy (TROSY) on NMR as a technique in structural biology. Q. Rev. Biophys. 33, 161-197.
18. Langer, T., Vogtherr, M., Elshorst, B., Betz, M., Schieborr, U., Saxena, K., and Schwalbe, H. (2004) NMR backbone assignment of a protein kinase catalytic domain by a combination of several approaches: application to the catalytic subunit of cAMP-dependent protein kinase. ChemBioChem 5, 1508-1516. (Pubitemid 39531664)
19. Zhang, F., Strand, A., Robbins, D., Cobb, M. H., and Goldsmith, E. J. (1994) Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature 367, 704-711.
20. Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., and Goldsmith, E. J. (1997) Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90, 859-869. (Pubitemid 27381625)
21. Shen, Y., and Bax, A. (2007) Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology. J. Biomol. NMR 38, 289-302. (Pubitemid 47108511)
22. Fushman, D., Xu, R., and Cowburn, D. (1999) Direct determination of changes of interdomain orientation on ligation: use of the orientational dependence of 15N NMR relaxation in Abl SH(32). Biochemistry 38, 10225-10230.
23. Piserchio, A., Nair, P. A., Shuman, S., and Ghose, R. (2010) Solution NMR studies of Chlorella virus DNA ligase-adenylate. J. Mol. Biol. 395, 291-308.
24. Wüthrich, K. (1986) NMR of proteins and nucleic acids, John Wiley and Sons, New York.
25. Muchmore, D. C., McIntosh, L. P., Russell, C. B., Anderson, D. E., and Dahlquist, F. W. (1989) Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Meth. Ezymnol. 177, 44-73. (Pubitemid 20041570)
26. Englander, J., Cohen, L., Arshava, B., Estephan, R., Becker, J. M., and Naider, F. (2006) Selective labeling of a membrane peptide with 15N-amino acids using cells grown in rich medium. Biopolymers 84, 508-518. (Pubitemid 44519210)
27. LeMaster, D. M., and Cronan, J. E., Jr. (1982) Biosynthetic production of 13 C-labeled amino acids with site-specific enrichment. J. Biol. Chem. 257, 1224-1230.
28. Takeuchi, K., Ng, E., Malia, T. J., and Wagner, G. (2007) 1-13 C amino acid selective labeling in a 2 H 15N background for NMR studies of large proteins. J. Biomol. NMR 38, 89-98. (Pubitemid 46745446)
29. Vogel-Claude, P., Schafer, G., and Trommer, W. E. (1988) Synthesis of a photoaffinity-spinlabeled derivative of ATP and its first application to F1-ATPase. FEBS Lett. 227, 107-109. (Pubitemid 18033859)
30. Prowse, C. N., and Lew, J. (2001) Mechanism of activation of ERK2 by dual phosphorylation. J. Biol. Chem. 276, 99-103. (Pubitemid 32050294)
31. Li, Y., and Palmer, A. G., III. (2010) Narrowing of protein NMR spectral lines broadened by chemical exchange. J. Am. Chem. Soc. 132, 8856-8857.
32. Piserchio, A., Warthaka, M., Devkota, A. K., Kaoud, T. S., Lee, S., Abramczyk, O., Ren, P., Dalby, K. N., and Ghose R. (2011) Solution NMR insights into docking interactions involving inactive ERK2. Biochemistry, 50, 3660-3672.