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Volumn 1784, Issue 9, 2008, Pages 1208-1214

Structural characterisation of PinA WW domain and a comparison with other Group IV WW domains, Pin1 and Ess1

Author keywords

Molecular dynamics; NMR; Protein structure; Structure comparison; WW domain

Indexed keywords

ARTICLE; ASPERGILLUS NIDULANS; HYDROPHOBICITY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; CANDIDA ALBICANS; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYMOLOGY; GENETICS; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; THERMODYNAMICS;

EID: 53149141784     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.04.026     Document Type: Article
Times cited : (6)

References (47)
  • 1
    • 0033900164 scopus 로고    scopus 로고
    • Converging on proline: The mechanism of WW domain peptide recognition
    • A. Zarrinpar, W.A. Lim, Converging on proline: the mechanism of WW domain peptide recognition, Nat. Struct. Biol. 7 (2000) 611-613.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 611-613
    • Zarrinpar, A.1    Lim, W.A.2
  • 4
    • 0037155792 scopus 로고    scopus 로고
    • Determinants of ligand specificity in Groups I and IV WW domains as studied by surface plasmon resonance and model building
    • Y. Kato, M. Ito, K. Kawai, K. Nagata, M. Tanokura, Determinants of ligand specificity in Groups I and IV WW domains as studied by surface plasmon resonance and model building, J. Biol. Chem. 277 (2002) 10173-10177.
    • (2002) J. Biol. Chem , vol.277 , pp. 10173-10177
    • Kato, Y.1    Ito, M.2    Kawai, K.3    Nagata, K.4    Tanokura, M.5
  • 5
    • 3843151562 scopus 로고    scopus 로고
    • redefining their functional classification
    • Common mechanism of ligand recognition by Group II/III WW domains
    • Y. Kato, K. Nagata, M. Takahashi, L. Lian, J.J. Herrero, M. Sudol, M. Tanokura, Common mechanism of ligand recognition by Group II/III WW domains: redefining their functional classification, J. Biol. Chem. 279 (2004) 31833-31841.
    • (2004) J. Biol. Chem , vol.279 , pp. 31833-31841
    • Kato, Y.1    Nagata, K.2    Takahashi, M.3    Lian, L.4    Herrero, J.J.5    Sudol, M.6    Tanokura, M.7
  • 7
    • 0033629682 scopus 로고    scopus 로고
    • Phosphorylation-dependent prolyl isomerization: A novel cell cycle regulatory mechanism
    • K.P. Lu, Phosphorylation-dependent prolyl isomerization: a novel cell cycle regulatory mechanism, Prog. Cell Cycle Res. 4 (2000) 83-96.
    • (2000) Prog. Cell Cycle Res , vol.4 , pp. 83-96
    • Lu, K.P.1
  • 8
    • 0032926319 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
    • S.F. Gothel, M.A. Marahiel, Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts, Cell. Mol. Life Sci. 55 (1999) 423-436.
    • (1999) Cell. Mol. Life Sci , vol.55 , pp. 423-436
    • Gothel, S.F.1    Marahiel, M.A.2
  • 10
    • 2942616943 scopus 로고    scopus 로고
    • Genetic interactions with C-terminal domain (CTD) kinases and the CTD of RNA PolII suggest a role for ESS1 in transcription and elongation in Saccharomyces cerevisiae
    • C.B. Wilcox, A. Rossettini, S.D. Hanes, Genetic interactions with C-terminal domain (CTD) kinases and the CTD of RNA PolII suggest a role for ESS1 in transcription and elongation in Saccharomyces cerevisiae, Genetics 167 (2004) 93-105.
    • (2004) Genetics , vol.167 , pp. 93-105
    • Wilcox, C.B.1    Rossettini, A.2    Hanes, S.D.3
  • 11
    • 0347361694 scopus 로고    scopus 로고
    • The ESS1 prolyl isomerase and its suppressor BYE1 interact with RNA pol II to inhibit transcription elongation in Saccharomyces cerevisiae
    • X. Wu, A. Rossettini, S.D. Hanes, The ESS1 prolyl isomerase and its suppressor BYE1 interact with RNA pol II to inhibit transcription elongation in Saccharomyces cerevisiae, Genetics 165 (2003) 1687-1702.
    • (2003) Genetics , vol.165 , pp. 1687-1702
    • Wu, X.1    Rossettini, A.2    Hanes, S.D.3
  • 12
    • 0033885803 scopus 로고    scopus 로고
    • Structural basis for phosphoserine-proline recognition by group IV WW domains
    • M.A. Verdecia, M.E. Bowman, K.P. Lu, T. Hunter, J.P. Noel, Structural basis for phosphoserine-proline recognition by group IV WW domains, Nat. Struct. Biol. 7 (2000) 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
  • 13
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • R. Ranganathan, K.P. Lu, T. Hunter, J.P. Noel, Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent, Cell 89 (1997) 875-886.
    • (1997) Cell , vol.89 , pp. 875-886
    • Ranganathan, R.1    Lu, K.P.2    Hunter, T.3    Noel, J.P.4
  • 14
    • 34548225350 scopus 로고    scopus 로고
    • PinA from Aspergillus nidulans binds to pS/pT-P motifs using the same Loop I and XP groove as mammalian Pin1
    • Y. Kato, C.A. Ng, R.T.C. Brownlee, M. Tanokura, PinA from Aspergillus nidulans binds to pS/pT-P motifs using the same Loop I and XP groove as mammalian Pin1, Biochim. Biophys. Acta 1774 (2007) 1208-1212.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 1208-1212
    • Kato, Y.1    Ng, C.A.2    Brownlee, R.T.C.3    Tanokura, M.4
  • 15
    • 34247180580 scopus 로고    scopus 로고
    • Sequence-specific dynamics modulate recognition specificity in WW domains
    • T. Peng, J.S. Zintsmaster, A.T. Namanja, J.W. Peng, Sequence-specific dynamics modulate recognition specificity in WW domains, Nat. Struct. Mol. Biol. 14 (2007) 325-331.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 325-331
    • Peng, T.1    Zintsmaster, J.S.2    Namanja, A.T.3    Peng, J.W.4
  • 16
    • 34250793476 scopus 로고    scopus 로고
    • Influence of hPin1 WW N-terminal domain boundaries on function, protein stability, and folding
    • M. Jager, H. Nguyen, M. Dendle, M. Gruebele, J.W. Kelly, Influence of hPin1 WW N-terminal domain boundaries on function, protein stability, and folding, Protein sci. 16 (2007) 1495-1501.
    • (2007) Protein sci , vol.16 , pp. 1495-1501
    • Jager, M.1    Nguyen, H.2    Dendle, M.3    Gruebele, M.4    Kelly, J.W.5
  • 18
    • 0038342514 scopus 로고    scopus 로고
    • Peptide binding induces large scale changes in inter-domain mobility in human Pin1
    • D.M. Jacobs, K. Saxena, M. Vogtherr, P. Bernado, M. Pons, K.M. Fiebig, Peptide binding induces large scale changes in inter-domain mobility in human Pin1, J. Biol. Chem. 278 (2003) 26174-26182.
    • (2003) J. Biol. Chem , vol.278 , pp. 26174-26182
    • Jacobs, D.M.1    Saxena, K.2    Vogtherr, M.3    Bernado, P.4    Pons, M.5    Fiebig, K.M.6
  • 19
    • 0038448924 scopus 로고    scopus 로고
    • Structural analysis of the mitotic regulator hPin1 in solution: Insights into domain architecture and substrate binding
    • E. Bayer, S. Goettsch, J.W. Mueller, B. Griewel, E. Guiberman, L.M. Mayr, P. Bayer, Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding, J. Biol. Chem. 278 (2003) 26183-26193.
    • (2003) J. Biol. Chem , vol.278 , pp. 26183-26193
    • Bayer, E.1    Goettsch, S.2    Mueller, J.W.3    Griewel, B.4    Guiberman, E.5    Mayr, L.M.6    Bayer, P.7
  • 21
    • 85030579971 scopus 로고    scopus 로고
    • T.D. Goddard, D.G. Kneller, SPARKY3, (University of California, San Francisco).
    • T.D. Goddard, D.G. Kneller, SPARKY3, (University of California, San Francisco).
  • 23
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • G. Cornilescu, F. Delaglio, A. Bax, Protein backbone angle restraints from searching a database for chemical shift and sequence homology, J. Biomol. NMR 13 (1999) 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 24
    • 0021764813 scopus 로고
    • Calibration of the angular dependence of the amide proton-Ca proton coupling constants
    • A. Pardi, M. Billeter, K. Wuthrich, Calibration of the angular dependence of the amide proton-Ca proton coupling constants, J. Mol. Biol. 180 (1984) 741-751.
    • (1984) J. Mol. Biol , vol.180 , pp. 741-751
    • Pardi, A.1    Billeter, M.2    Wuthrich, K.3
  • 25
    • 12044259775 scopus 로고    scopus 로고
    • G.W. Vuister, A. Bax, Quantitative J correlation: a new approach for measuring homonuclear three-bond J(HN-H{alpha}) coupling constants in 15N-enriched proteins, J. Am. Chem. Soc. 115 (1993) 7772-7777.
    • G.W. Vuister, A. Bax, Quantitative J correlation: a new approach for measuring homonuclear three-bond J(HN-H{alpha}) coupling constants in 15N-enriched proteins, J. Am. Chem. Soc. 115 (1993) 7772-7777.
  • 26
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
    • D.S. Wishart, B.D. Sykes, The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data, J. Biomol. NMR 4 (1994) 171-180.
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 27
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • P. Güntert, C. Mumenthaler, K. Wuthrich, Torsion angle dynamics for NMR structure calculation with the new program DYANA, J. Mol. Biol. 273 (1997) 283-298.
    • (1997) J. Mol. Biol , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 28
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • T. Herrmann, P. Güntert, K. Wüthrich, Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA, J. Mol. Biol. 319 (2002) 209-227.
    • (2002) J. Mol. Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 29
    • 85030589242 scopus 로고    scopus 로고
    • D.A. Case, T.A. Darden, I. Cheatham, T.E., C.L. Simmerling, J. Wang, R.E. Duke, R. Luo, K.M. Merz, D.A. Pearlman, M. Crowley, R.C. Walker, W. Zhang, B. Wang, S. Hayik, A. Roitberg, G. Seabra, K.F. Wong, F. Paesani, X. Wu, S. Brozell, V. Tsui, H. Gohlke, L. Yang, C. Tan, J. Mongan, V. Hornak, G. Cui, P. Beroza, D.H. Mathews, C. Schafmeister, W.S. Ross, P.A. Kollman, AMBER 9, University of California, San Francisco, 2006.
    • D.A. Case, T.A. Darden, I. Cheatham, T.E., C.L. Simmerling, J. Wang, R.E. Duke, R. Luo, K.M. Merz, D.A. Pearlman, M. Crowley, R.C. Walker, W. Zhang, B. Wang, S. Hayik, A. Roitberg, G. Seabra, K.F. Wong, F. Paesani, X. Wu, S. Brozell, V. Tsui, H. Gohlke, L. Yang, C. Tan, J. Mongan, V. Hornak, G. Cui, P. Beroza, D.H. Mathews, C. Schafmeister, W.S. Ross, P.A. Kollman, AMBER 9, University of California, San Francisco, 2006.
  • 31
    • 0031834850 scopus 로고    scopus 로고
    • Importance of explicit salt ions for protein stability in molecular dynamics simulation
    • G.T. Ibragimova, R.C. Wade, Importance of explicit salt ions for protein stability in molecular dynamics simulation, Biophys. J. 74 (1998) 2906-2911.
    • (1998) Biophys. J , vol.74 , pp. 2906-2911
    • Ibragimova, G.T.1    Wade, R.C.2
  • 33
    • 11144243217 scopus 로고    scopus 로고
    • Hydrogen exchange and ligand binding: Ligand-dependent and ligand-independent protection in the Src SH3 domain
    • D. Wildes, S. Marqusee, Hydrogen exchange and ligand binding: Ligand-dependent and ligand-independent protection in the Src SH3 domain, Protein sci. 14 (2005) 81-88.
    • (2005) Protein sci , vol.14 , pp. 81-88
    • Wildes, D.1    Marqusee, S.2
  • 34
    • 33747631086 scopus 로고    scopus 로고
    • Study of structural stability of cyclophilin A by NMR and circular dechroism spectra
    • Y.H. Shi, D.H. Lin, J.Y. Huang, X. Shen, Study of structural stability of cyclophilin A by NMR and circular dechroism spectra, Chin. J. Chem. 24 (2006) 973-979.
    • (2006) Chin. J. Chem , vol.24 , pp. 973-979
    • Shi, Y.H.1    Lin, D.H.2    Huang, J.Y.3    Shen, X.4
  • 35
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • A. Hvidt, S.O. Nielsen, Hydrogen exchange in proteins, Adv. Protein Chem. 21 (1966) 287-386.
    • (1966) Adv. Protein Chem , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 36
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of protein and nucleic acids
    • S.W. Englander, N.R. Kallenbach, Hydrogen exchange and structural dynamics of protein and nucleic acids, Quart. Rev. Biophys. 16 (1984) 521-655.
    • (1984) Quart. Rev. Biophys , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 37
    • 0023046606 scopus 로고
    • Two-dimensional 1H-NMR studies of cytochrome c: Hydrogen exchange in the N-terminal helix
    • A.J. Wand, H. Roder, S.W. Englander, Two-dimensional 1H-NMR studies of cytochrome c: hydrogen exchange in the N-terminal helix, Biochemistry 25 (1986) 1107-1114.
    • (1986) Biochemistry , vol.25 , pp. 1107-1114
    • Wand, A.J.1    Roder, H.2    Englander, S.W.3
  • 38
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Y. Bai, J.S. Milne, L. Mayne, S.W. Englander, Primary structure effects on peptide group hydrogen exchange, Proteins 17 (1993) 75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 40
    • 0000243829 scopus 로고
    • a program to check the stereochemical quality of protein structures
    • PROCHECK
    • R.A. Laskowski, M.W. MacArthur, D.S. Moss, J.M. Thornton, PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26 (1993) 283-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 41
    • 3042848873 scopus 로고    scopus 로고
    • Context-dependent contributions of backbone hydrogen bonding to beta-sheet folding energetics
    • S. Deechongkit, H. Nguyen, E.T. Powers, P.E. Dawson, M. Gruebele, J.W. Kelly, Context-dependent contributions of backbone hydrogen bonding to beta-sheet folding energetics, Nature 430 (2004) 101-105.
    • (2004) Nature , vol.430 , pp. 101-105
    • Deechongkit, S.1    Nguyen, H.2    Powers, E.T.3    Dawson, P.E.4    Gruebele, M.5    Kelly, J.W.6
  • 42
    • 33646396797 scopus 로고    scopus 로고
    • Expression and purification of active WW domains of FBP11/HYPA and FBP28/CA150
    • Y. Kato, Y. Sawano, M. Tanokura, Expression and purification of active WW domains of FBP11/HYPA and FBP28/CA150, Protein Pept. Lett. 13 (2006) 197-201.
    • (2006) Protein Pept. Lett , vol.13 , pp. 197-201
    • Kato, Y.1    Sawano, Y.2    Tanokura, M.3
  • 43
    • 17644385551 scopus 로고    scopus 로고
    • The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility
    • Z. Li, H. Li, G. Devasahayam, T. Gemmill, V. Chaturvedi, S.D. Hanes, P. Van Roey, The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility, Biochemistry 44 (2005) 6180-6189.
    • (2005) Biochemistry , vol.44 , pp. 6180-6189
    • Li, Z.1    Li, H.2    Devasahayam, G.3    Gemmill, T.4    Chaturvedi, V.5    Hanes, S.D.6    Van Roey, P.7
  • 45
    • 0343081091 scopus 로고    scopus 로고
    • Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan
    • X. Huang, F. Poy, R. Zhang, A. Joachimiak, M. Sudol, M.J. Eck, Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan, Nat. Struct. Biol. 7 (2000) 634-638.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 634-638
    • Huang, X.1    Poy, F.2    Zhang, R.3    Joachimiak, A.4    Sudol, M.5    Eck, M.J.6
  • 46
    • 33845999306 scopus 로고    scopus 로고
    • Structure of a FBP11 WW1-PL ligand complex reveals the mechanism of proline-rich ligand recognition by group-II/III WW domains
    • Y. Kato, T. Miyakawa, J.I. Kurita, M. Tanokura, Structure of a FBP11 WW1-PL ligand complex reveals the mechanism of proline-rich ligand recognition by group-II/III WW domains, J. Biol. Chem. 281 (2006) 40321-40329.
    • (2006) J. Biol. Chem , vol.281 , pp. 40321-40329
    • Kato, Y.1    Miyakawa, T.2    Kurita, J.I.3    Tanokura, M.4
  • 47
    • 0036928101 scopus 로고    scopus 로고
    • Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40
    • S. Wiesner, G. Stier, M. Sattler, M.J. Macias, Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40, J. Mol. Biol. 324 (2002) 807.
    • (2002) J. Mol. Biol , vol.324 , pp. 807
    • Wiesner, S.1    Stier, G.2    Sattler, M.3    Macias, M.J.4


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