Influence of hPin1 WW N-terminal domain boundaries on function, protein stability, and folding

Protein Science

Volumn 16, Issue 7, 2007, Pages 1495-1501

  Jager, Marcus ^a,c   Nguyen, Houbi ^b,d   Dendle, Maria ^a   Gruebele, Martin ^b   Kelly, Jeffery W ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d STANFORD UNIVERSITY   (United States)

Author keywords

sheet; Domain boundaries; Double mutant cycle analysis; Laser temperature jump relaxation; Protein stability; WW domain

Indexed keywords

AMMONIA; ION; PEPTIDYLPROLYL ISOMERASE PIN1;

AMINO TERMINAL SEQUENCE; ARTICLE; FUNGUS; LASER; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; THERMODYNAMICS; X RAY; YEAST;

AMINO ACID SEQUENCE; CATALYSIS; CATALYTIC DOMAIN; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDYLPROLYL ISOMERASE; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; THERMODYNAMICS;

FUNGI;

EID: 34250793476     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.072775507     Document Type: Article

References (29)

1. Cecconi, F., Guardiani, C., and Livi, R. 2006. Testing simplified proteins models of the hPin1 WW domain. Biophys. J. 91: 694-704.
2. Cheung, M.S., Klimov, D., and Thirumalai, D. 2005. Molecular crowding enhances native state stability and refolding rates of globular proteins. Proc. Natl. Acad. Sci. 102: 4753-4758.
3. Crane, J.C., Koepf, E.K., Kelly, J.W., and Gruebele, M. 2000. Mapping the transition state of the WW domain β-sheet. J. Mol. Biol. 298: 283-292.
4. Deechongkit, S. and Kelly, J.W. 2002. The effect of backbone cyclization on the thermodynamics of β-sheet unfolding: Stability optimization of the PIN WW domain. J. Am. Chem. Soc. 124: 4980-4986.
5. Deechongkit, S., Nguyen, H., Jager, M., Powers, E.T., Gruebele, M., and Kelly, J.W. 2006. β-sheet folding mechanisms from perturbation energetics. Curr. Opin. Struct. Biol. 16: 94-101.
6. Deechongkit, S., Nguyen, H., Powers, E.T., Dawson, P.E., Gruebele, M., and Kelly, J.W. 2004. Context-dependent contributions of backbone hydrogen bonding to b-sheet folding energetics. Nature 430: 101-105.
7. Fersht, A.R. and Sato, S. 2004. -value analysis and the nature of protein-folding transition states. Proc. Natl. Acad. Sci. 101: 7976-7981.
8. Horovitz, A. 1996. Double mutant cycles: A powerful tool for analyzing protein structure and function. Fold. Des. 1: R121-R126.
9. Hu, H., Columbus, J., Zhang, Y., Wu, D., Lian, L., Yang, S., Goodwin, J., Luczak, C., Carter, M., Chen, L., et al. 2004. A map of WW domain family interactions. Proteomics 4: 643-655.
10. Huang, X., Poy, F., Zhang, R., Joachimiak, A., Sudol, M., and Eck, M.J. 2000. Structure of a WW domain containing fragment of dystrophin in complex with β-dystroglycan. Nat. Struct. Biol. 7: 634-638.
11. Jäger, M., Nguyen, H., Crane, J.C., Kelly, J.W., and Gruebele, M. 2001. The folding mechanism of a β-sheet: The WW domain. J. Mol. Biol. 311: 373-393.
12. Jäger, M., Zhang, Y., Bieschke, J., Nguyen, H., Dendle, M., Bowman, M.E., Noel, J.P., Gruebele, M., and Kelly, J.W. 2006. Structure-function-folding relationship in a WW domain. Proc. Natl. Acad. Sci. 103: 10648-10653.
13. Kaul, R., Angeles, A.R., Jager, J., Powers, E.T., and Kelly, J.W. 2001. Incorporating β-turns and a turn mimetic out of context in loop 1 of the WW domain affords cooperatively folded β-sheets. J. Am. Chem. Soc. 123: 5206-5212.
14. Kowalski, J.A., Liu, K., and Kelly, J.W. 2002. NMR solution structure of the isolated Apo Pin1 WW domain: Comparison to the X-ray crystal structures of Pin1. Biopolymers 63: 111-121.
15. Macias, M.J., Hyvonen, M., Baraldi, E., Schultz, J., Sudol, M., Saraste, M., and Oschkinat, H. 1996. Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature 382: 646-649.
16. Macias, M.J., Gervais, V., Civera, C., and Oschkinat, H. 2000. Structural analysis of WW domains and design of a WW prototype. Nat. Struct. Biol. 7: 375-379.
17. Nguyen, H., Jager, M., Kelly, J.W., and Gruebele, M. 2005. Engineering a β-sheet protein toward the folding speed limit. J. Phys. Chem. B 109: 15182-15186.
18. Petrovich, M., Jonsson, A.L., Ferguson, N., Deggett, V., and Fersht, A.R. 2006. Phi-analysis at the experimental limits: Mechanism of β-hairpin formation. J. Mol. Biol. 360: 865-881.
19. Pires, J.R., Taha-Nejad, F., Toepert, F., Ast, T., Hoffmuller, U., Schneider-Mergener, J., Kuhne, R., Marcias, M.J., and Oschkinat, H. 2001. Solution structures of the YAP65 WW domain and the variant L30 K in complex with the peptides GTPPPPYTVG, N-(n-octyl)-GPPPY and PLPPY and the application of peptide libraries reveal a minimal binding epitope. J. Mol. Biol. 314: 1147-1156.
20. Powers, E.T., Deechongkit, S., and Kelly, J.W. 2005. Backbone-backbone H-bonds make context-dependent contributions to protein folding kinetics and thermodynamics: Lessons from amide-to-ester mutations. Adv. Protein Chem. 72: 39-78.
21. Ranganathan, R., Lu, K.P., Hunter, T., and Noel, J.P. 1997. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell 89: 875-886.
22. Russ, W.P., Lowery, D.M., Mishra, P., Yaffe, M.B., and Ranganathan, R. 2005. Natural-like function in artificial WW domains. Nature 437: 579-583.
23. Socolich, M., Lockless, S.W., Russ, W.P., Lee, H., Gardner, K.H., and Ranganathan, R. 2005. Evolutionary information for specifying a protein fold. Nature 437: 512-518.
24. Sudol, M. 1996. Structure and function of the WW domain. Prog. Biophys. Mol. Biol. 65: 113-132.
25. Sudol, M., Chen, H.I., Bougeret, C., Einbond, A., and Bork, P. 1995. Characterization of a novel protein-binding module - The WW domain. FEBS Lett. 369: 67-71.
26. Verdecia, M.A., Bowman, M.E., Lu, K.P., Hunter, T., and Noel, J.P. 2000. Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat. Struct. Biol. 7: 639-643.
27. Wells, J.A. 1990. Additivity of mutational effects in proteins. Biochemistry 29: 8509-8517.
28. Wiesner, S., Stier, G., Sattler, M., and Macias, M.J. 2002. Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40. J. Mol. Biol. 324: 807-822.
29. Zhou, H.X. 2003. Effect of backbone cyclization on protein folding stability: Chain entropies of both the unfolded and the folded states are restricted. J. Mol. Biol. 332: 257-264.