Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain

Protein Science

Volumn 15, Issue 1, 2006, Pages 162-170

  Zarrine Afsar, Arash ^a   Mittermaier, Anthony ^a   Kay, Lewis E ^a,b   Davidson, Alan R ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

Arginine protein interaction; Guanidinium induced protein stabilization; Peptide binding; Protein folding kinetics; SH3 domain; Specific guanidinium binding

Indexed keywords

ARGININE; GUANIDINE; PROTEIN SH3; SODIUM CHLORIDE;

ARTICLE; BAY REGION BINDING SITE; DISSOCIATION CONSTANT; ENERGY TRANSFER; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SURFACE PROPERTY; THERMODYNAMICS; THERMOSTABILITY;

ANIMALS; ARGININE; BINDING SITES; GUANIDINE; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MUTATION; PEPTIDES; PROTEIN BINDING; PROTEIN DENATURATION; PROTO-ONCOGENE PROTEINS C-FYN; SODIUM CHLORIDE; SRC HOMOLOGY DOMAINS; SURFACE PROPERTIES; THERMODYNAMICS; UREA;

EID: 29344434301     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.051829106     Document Type: Article

References (33)

1. Bhuyan, A.K. 2002. Protein stabilization by urea and guanidine hydrochloride. Biochemistry 41: 13386-13394.
2. Bogan, A.A. and Thorn, K.S. 1998. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280: 1-9.
3. Collins, K.D. 2004. Ions from the Hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process. Methods 34: 300-311.
4. de Los Rios, M.A. and Plaxco, K.W. 2005. Apparent Debye-Huckel electrostatic effects in the folding of a simple, single domain protein. Biochemistry 44: 1243-1250.
5. Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
6. Di Nardo, A.A., Korzhnev, D.M., Stogios, P.J., Zarrine-Afsar, A., Kay, L.E., and Davidson, A.R. 2004. Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformation. Proc. Natl. Acad. Sci. 101: 7954-7959.
7. Dunbar, J., Yennawar, H.P., Banerjee, S., Luo, J., and Farber, G.K. 1997. The effect of denaturants on protein structure. Protein Sci. 6: 1727-1733.
8. Efron, B. and Tibshirani, R. 1986. Bootstrap methods for standard errors, confidence intervals and other measures of statistical accuracy. Stat. Sci. 1: 54-77.
9. Fazi, B., Cope, M.J., Douangamath, A., Ferracuti, S., Schirwitz, K., Zucconi, A., Drubin, D.G., Wilmanns, M., Cesareni, G., and Castagnoli, L. 2002. Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: Structural and functional analysis. J. Biol. Chem. 277: 5290-5298.
10. Feng, S., Kasahara, C., Rickles, R.J., and Schreiber, S.L. 1995. Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands. Proc. Natl. Acad. Sci. 92: 12408-12415.
11. Jones, S. and Thornton, J.M. 1996. Principles of protein-protein interactions. Proc. Natl. Acad. Sci. 93: 13-20.
12. Kay, L.E., Keifer, P., and Saarinen, T. 1992. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114: 10663-10665.
13. Koradi, R., Billeter, M., and Wuthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14: 51-55.
14. Logan, T.M., Olejniczak, E.T., Xu, R.X., and Fesik, S.W. 1993. A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments. J. Biomol. NMR 3: 225-231.
15. Makhatadze, G.I. 1999. Thermodynamics of protein interactions with Urea and Guanidinium Hydrochloride. J. Phys. Chem. B 103: 4781-4785.
16. Makhatadze, G.I. and Privalov, P.L. 1992. Protein interactions with urea and guanidinium chloride. A calorimetric study. J.Mol. Biol. 226: 491-505.
17. Makhatadze, G.I., Lopez, M.M., Richardson 3rd, J.M., and Thomas, S.T. 1998. Anion binding to the ubiquitin molecule. Protein Sci. 7: 689-697.
18. Marles, J.A., Dahesh, S., Haynes, J., Andrews, B.J., and Davidson, A.R. 2004. Protein-protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast. Mol. Cell 14: 813-823.
19. Maxwell, K.L. and Davidson, A.R. 1998. Mutagenesis of a buried polar interaction in an SH3 domain: Sequence conservation provides the best prediction of stability effects. Biochemistry 37: 16172-16182.
20. Mayr, L.M. and Schmid, F.X. 1993. Stabilization of a protein by guanidinium chloride. Biochemistry 32: 7994-7998.
21. Moglich, A., Krieger, F., and Kiefhaber, T. 2005. Molecular basis for the effect of urea and guanidinium chloride on the dynamics of unfolded polypeptide chains. J. Mol. Biol. 345: 153-162.
22. Monera, O.D., Kay, C.M., and Hodges, R.S. 1994. Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3: 1984-1991.
23. Montelione, G.T., Lyons, B.A., Emerson, S.D., and Tashiro, M. 1992. An efficient triple resonance experiment using carbon 13 isotropic mixing for determining sequence-specific resonance assignments of isotopically-enriched proteins. J. Am. Chem. Soc. 114: 10974-10975.
24. Noble, M.E., Musacchio, A., Saraste, M., Courtneidge, S.A., and Wierenga, R.K. 1993. Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin. EMBO J. 12: 2617-2624.
25. Northey, J.G., Di Nardo, A.A., and Davidson, A.R. 2002. Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9: 126-130.
26. Rath, A. and Davidson, A.R. 2000. The design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysis. Protein Sci. 9: 2457-2469.
27. Rickles, R.J., Botfield, M.C., Zhou, X.M., Henry, P.A., Brugge, J.S., and Zoller, M.J. 1995. Phage display selection of ligand residues important for Src homology 3 domain binding specificity. Proc. Natl. Acad. Sci. 92: 10909-10913.
28. Sanchez, I.E. and Kiefhaber, T. 2003. Hammond behavior versus ground state effects in protein folding: Evidence for narrow free energy barriers and residual structure in unfolded states. J. Mol. Biol. 327: 867-884.
29. Schellman, J.A. 2002. Fifty years of solvent denaturation. Biophys. Chem. 96: 91-101.
30. 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR 6: 135-140.
31. Wittekind, M. and Mueller, L. 1993. HNCACB, a high sensitivity 3D NMR experiment to correlate amide proton and nitrogen resonances with the α- and β-carbon resonances in proteins. J. Magn. Reson. Series B 101: 201-205.
32. Yousef, M.S., Baase, W.A., and Matthews, B.W. 2004. Use of sequence duplication to engineer a ligand-triggered, long-distance molecular switch in T4 lysozyme. Proc. Natl. Acad. Sci. 101: 11583-11586.
33. Zarrinpar, A., Bhattacharyya, R.P., Nittler, M.P., and Lim, W.A. 2004. Sho1 and Pbs2 act as coscaffolds linking components in the yeast high osmolarity MAP kinase pathway. Mol. Cell 14: 825-832.