메뉴 건너뛰기




Volumn 16, Issue 10, 2007, Pages 2306-2313

A cross-strand Trp-Trp pair stabilizes the hPin1 WW domain at the expense of function

Author keywords

sheet; Protein engineering; Secondary structure propensity; Trp zipper; WW domain

Indexed keywords

HYDROGEN; INDOLE; LIGAND; MUTANT PROTEIN; PEPTIDYLPROLYL ISOMERASE PIN1; TRYPTOPHAN;

EID: 34748874234     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.072904107     Document Type: Article
Times cited : (42)

References (38)
  • 2
    • 0041866611 scopus 로고    scopus 로고
    • Stabilization of β-hairpin peptides by salt bridges: Role of preorganization in the energetic contribution of weak interactions
    • Ciani, B., Jourdan, M., and Searle, M.S. 2003. Stabilization of β-hairpin peptides by salt bridges: Role of preorganization in the energetic contribution of weak interactions. J. Am. Chem. Soc. 125: 9038-9047.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 9038-9047
    • Ciani, B.1    Jourdan, M.2    Searle, M.S.3
  • 5
    • 0034724566 scopus 로고    scopus 로고
    • Mapping the transition state of the WW domain β-sheet
    • 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.
    • (2000) J. Mol. Biol , vol.298 , pp. 283-292
    • Crane, J.C.1    Koepf, E.K.2    Kelly, J.W.3    Gruebele, M.4
  • 6
    • 0031454065 scopus 로고    scopus 로고
    • Cross-strand side-chain interactions versus turn conformation in β-hairpins
    • de Alba, E., Rico, M., and Jiménez, M.A. 1997. Cross-strand side-chain interactions versus turn conformation in β-hairpins. Protein Sci. 6: 2548-2560.
    • (1997) Protein Sci , vol.6 , pp. 2548-2560
    • de Alba, E.1    Rico, M.2    Jiménez, M.A.3
  • 7
    • 0037042295 scopus 로고    scopus 로고
    • The effect of backbone cyclization on the thermodynamics of β-sheet unfolding: Stability optimization of the PIN WW domain
    • 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.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 4980-4986
    • Deechongkit, S.1    Kelly, J.W.2
  • 8
    • 33644516904 scopus 로고    scopus 로고
    • Understanding the mechanism of β-hairpin folding via φ-value analysis
    • Du, D., Tucker, M.J., and Gai, F. 2006. Understanding the mechanism of β-hairpin folding via φ-value analysis. Biochemistry 45: 2668-2678.
    • (2006) Biochemistry , vol.45 , pp. 2668-2678
    • Du, D.1    Tucker, M.J.2    Gai, F.3
  • 10
    • 0032246263 scopus 로고    scopus 로고
    • Minimal model systems for b sheet secondary structure in proteins
    • Gellman, S.H. 1998. Minimal model systems for b sheet secondary structure in proteins. Curr. Opin. Chem. Biol. 2: 717-725.
    • (1998) Curr. Opin. Chem. Biol , vol.2 , pp. 717-725
    • Gellman, S.H.1
  • 11
    • 0034691039 scopus 로고    scopus 로고
    • Long-range order in the src SH3 folding transition state
    • Grantcharova, V.P., Riddle, D.S., and Baker, D. 2000. Long-range order in the src SH3 folding transition state. Proc. Natl. Acad. Sci. 97: 7084-7089.
    • (2000) Proc. Natl. Acad. Sci , vol.97 , pp. 7084-7089
    • Grantcharova, V.P.1    Riddle, D.S.2    Baker, D.3
  • 12
    • 0018368942 scopus 로고
    • Kinetics of the helix-coil transition of a polypeptide with non-ionic side groups, derived from ultrasonic relaxation measurements
    • Gruenewald, B., Nicola, C.U., Lustig, A., Schwarz, G., and Klump, H. 1979. Kinetics of the helix-coil transition of a polypeptide with non-ionic side groups, derived from ultrasonic relaxation measurements. Biophys. Chem. 9: 137-147.
    • (1979) Biophys. Chem , vol.9 , pp. 137-147
    • Gruenewald, B.1    Nicola, C.U.2    Lustig, A.3    Schwarz, G.4    Klump, H.5
  • 13
    • 0030322783 scopus 로고    scopus 로고
    • Double-mutant cycles: A powerful tool for analyzing protein structure and function
    • Horovitz, A. 1996. Double-mutant cycles: A powerful tool for analyzing protein structure and function. Fold. Des. 1: R121-R126.
    • (1996) Fold. Des , vol.1
    • Horovitz, A.1
  • 16
    • 0034685619 scopus 로고    scopus 로고
    • A breakdown of symmetry in the folding transition state of protein L
    • Kim, D.E., Fisher, C., and Baker, D. 2000. A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298: 971-984.
    • (2000) J. Mol. Biol , vol.298 , pp. 971-984
    • Kim, D.E.1    Fisher, C.2    Baker, D.3
  • 17
    • 0033607151 scopus 로고    scopus 로고
    • Characterization of the structure and function of W → F WW domain variants: Identification of a natively unfolded protein that folds upon ligand binding
    • Koepf, E.K., Petrassi, H.M., Ratnaswamy, G., Huff, M.E., Sudol, M., and Kelly, J.W. 1999. Characterization of the structure and function of W → F WW domain variants: Identification of a natively unfolded protein that folds upon ligand binding. Biochemistry 38: 14338-14351.
    • (1999) Biochemistry , vol.38 , pp. 14338-14351
    • Koepf, E.K.1    Petrassi, H.M.2    Ratnaswamy, G.3    Huff, M.E.4    Sudol, M.5    Kelly, J.W.6
  • 18
    • 0036160702 scopus 로고    scopus 로고
    • NMR solution structure of the isolated Apo Pin1 WW domain: Comparison to the X-ray crystal structures of Pin1
    • 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.
    • (2002) Biopolymers , vol.63 , pp. 111-121
    • Kowalski, J.A.1    Liu, K.2    Kelly, J.W.3
  • 19
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • Macias, M.J., Wiesner, S., and Sudol, M. 2002. WW and SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Lett. 513: 30-37.
    • (2002) FEBS Lett , vol.513 , pp. 30-37
    • Macias, M.J.1    Wiesner, S.2    Sudol, M.3
  • 20
    • 0027998757 scopus 로고
    • Context is a major determinant of β-sheet propensity
    • Minor Jr., D.L. and Kim, P.S. 1994a. Context is a major determinant of β-sheet propensity. Nature 371: 264-267.
    • (1994) Nature , vol.371 , pp. 264-267
    • Minor Jr., D.L.1    Kim, P.S.2
  • 21
    • 0028176595 scopus 로고
    • Measurement of the β-sheet-forming propensities of amino acids
    • Minor Jr., D.L. and Kim, P.S. 1994b. Measurement of the β-sheet-forming propensities of amino acids. Nature 367: 660-663.
    • (1994) Nature , vol.367 , pp. 660-663
    • Minor Jr., D.L.1    Kim, P.S.2
  • 22
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • Munoz, V., Thompson, P.A., Hofrichter, J., and Eaton, W.A. 1997. Folding dynamics and mechanism of β-hairpin formation. Nature 390: 196-199.
    • (1997) Nature , vol.390 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 24
    • 0034964196 scopus 로고    scopus 로고
    • Computer-based redesign of a protein folding pathway
    • Nauli, S., Kuhlman, B., and Baker, D. 2001. Computer-based redesign of a protein folding pathway. Nat. Struct. Biol. 8: 602-605.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 602-605
    • Nauli, S.1    Kuhlman, B.2    Baker, D.3
  • 25
    • 0031558811 scopus 로고    scopus 로고
    • Role of β-turn residues in β-hairpin formation and stability in designed peptides
    • Ramirez-Alvarado, M., Blanco, F.J., Niemann, H., and Serrano, L. 1997. Role of β-turn residues in β-hairpin formation and stability in designed peptides. J. Mol. Biol. 273: 898-912.
    • (1997) J. Mol. Biol , vol.273 , pp. 898-912
    • Ramirez-Alvarado, M.1    Blanco, F.J.2    Niemann, H.3    Serrano, L.4
  • 26
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • 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.
    • (1997) Cell , vol.89 , pp. 875-886
    • Ranganathan, R.1    Lu, K.P.2    Hunter, T.3    Noel, J.P.4
  • 27
    • 0032317156 scopus 로고    scopus 로고
    • Deciphering rules of helix stability in peptides
    • Rohl, C.A. and Baldwin, R.L. 1998. Deciphering rules of helix stability in peptides. Methods Enzymol. 295: 1-26.
    • (1998) Methods Enzymol , vol.295 , pp. 1-26
    • Rohl, C.A.1    Baldwin, R.L.2
  • 28
    • 0034694688 scopus 로고    scopus 로고
    • Designing stable β-hairpins: Energetic contributions from cross-strand residues
    • Russell, S.J. and Cochran, A. 2001. Designing stable β-hairpins: Energetic contributions from cross-strand residues. J. Am. Chem. Soc. 122: 12600-12601.
    • (2001) J. Am. Chem. Soc , vol.122 , pp. 12600-12601
    • Russell, S.J.1    Cochran, A.2
  • 29
    • 0037438384 scopus 로고    scopus 로고
    • Stability of cyclic β-hairpins: Asymmetric contributions from side chains of a hydrogen-bonded cross-strand residue pair
    • Russell, S.J., Blandl, T., Skelton, N.J., and Cochran, A.G. 2003. Stability of cyclic β-hairpins: Asymmetric contributions from side chains of a hydrogen-bonded cross-strand residue pair. J. Am. Chem. Soc. 125: 388-395.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 388-395
    • Russell, S.J.1    Blandl, T.2    Skelton, N.J.3    Cochran, A.G.4
  • 30
    • 1842611349 scopus 로고    scopus 로고
    • Factors involved in the stability of isolated β-sheets: Turn sequence, β-sheet twisting, and hydrophobic surface burial
    • Santiveri, C.M., Santoro, J., Rico, M., and Jiménez, M.A. 2004. Factors involved in the stability of isolated β-sheets: Turn sequence, β-sheet twisting, and hydrophobic surface burial. Protein Sci. 13: 1134-1147.
    • (2004) Protein Sci , vol.13 , pp. 1134-1147
    • Santiveri, C.M.1    Santoro, J.2    Rico, M.3    Jiménez, M.A.4
  • 31
    • 78651171134 scopus 로고
    • On the kinetics of the helix-coil transition of polypeptides in solution
    • Schwarz, G. 1965. On the kinetics of the helix-coil transition of polypeptides in solution. J. Mol. Biol. 11: 64-77.
    • (1965) J. Mol. Biol , vol.11 , pp. 64-77
    • Schwarz, G.1
  • 32
    • 4143070403 scopus 로고    scopus 로고
    • Design of β-sheet systems for understanding the thermodynamics and kinetics of protein folding
    • Searle, M.S. and Ciani, B. 2004. Design of β-sheet systems for understanding the thermodynamics and kinetics of protein folding. Curr. Opin. Struct. Biol. 14: 458-464.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 458-464
    • Searle, M.S.1    Ciani, B.2
  • 33
    • 0028175780 scopus 로고
    • A thermodynamic scale for the β-sheet forming tendencies of the amino acids
    • Smith, C.K., Withka, J.M., and Regan, L. 1994. A thermodynamic scale for the β-sheet forming tendencies of the amino acids. Biochemistry 33: 5510-5517.
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 34
    • 0030424581 scopus 로고    scopus 로고
    • Structure and function of the WW domain
    • Sudol, M. 1996. Structure and function of the WW domain. Prog. Biophys. Mol. Biol. 65: 113-132.
    • (1996) Prog. Biophys. Mol. Biol , vol.65 , pp. 113-132
    • Sudol, M.1
  • 35
    • 0037436347 scopus 로고    scopus 로고
    • Influence of strand number on antiparallel β-sheet stability in designed three- and four-stranded β-sheets
    • Syud, F.A., Stanger, H.E., Mortell, H.S., Espinosa, J.F., Fisk, J.D., Fry, C.G., and Gellman, S.H. 2003. Influence of strand number on antiparallel β-sheet stability in designed three- and four-stranded β-sheets. J. Mol. Biol. 326: 553-568.
    • (2003) J. Mol. Biol , vol.326 , pp. 553-568
    • Syud, F.A.1    Stanger, H.E.2    Mortell, H.S.3    Espinosa, J.F.4    Fisk, J.D.5    Fry, C.G.6    Gellman, S.H.7
  • 36
    • 0037077578 scopus 로고    scopus 로고
    • Selective aromatic interactions in β-hairpin peptides
    • Tatko, C.D. and Waters, M.L. 2002. Selective aromatic interactions in β-hairpin peptides. J. Am. Chem. Soc. 124: 9372-9373.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 9372-9373
    • Tatko, C.D.1    Waters, M.L.2
  • 37
    • 0033885803 scopus 로고    scopus 로고
    • Structural basis for phosphoserine-proline recognition by group IV WW domains
    • 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.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 639-643
    • Verdecia, M.A.1    Bowman, M.E.2    Lu, K.P.3    Hunter, T.4    Noel, J.P.5
  • 38
    • 0000076259 scopus 로고
    • Determination of the parameters for helix formation in poly-γ-benzyl-L-glutamate
    • Zimm, B.H., Doty, P., and Iso, K. 1959. Determination of the parameters for helix formation in poly-γ-benzyl-L-glutamate. Proc. Natl. Acad. Sci. 45: 1601-1607.
    • (1959) Proc. Natl. Acad. Sci , vol.45 , pp. 1601-1607
    • Zimm, B.H.1    Doty, P.2    Iso, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.