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Volumn 335, Issue 4, 2004, Pages 1105-1115

Ligand-dependent Dynamics and Intramolecular Signaling in a PDZ Domain

Author keywords

Allostery; NMR; PDZ domain; Protein dynamics; Protein protein interaction

Indexed keywords

HUMAN TYROSINE PHOSPHATASE 1E; LIGAND; PDZ PROTEIN; PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 0347753736     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.11.010     Document Type: Article
Times cited : (198)

References (60)
  • 1
    • 0027383834 scopus 로고
    • Patterns of nonadditivity between pairs of stability mutations in Staphylococcal nuclease
    • Green S.M., Shortle D. Patterns of nonadditivity between pairs of stability mutations in Staphylococcal nuclease. Biochemistry. 32:1993;10131-10139.
    • (1993) Biochemistry , vol.32 , pp. 10131-10139
    • Green, S.M.1    Shortle, D.2
  • 2
    • 0035957014 scopus 로고    scopus 로고
    • The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin
    • Frauenfelder H., McMahon B.H., Austin R.H., Chu K., Groves J.T. The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin. Proc. Natl Acad. Sci. USA. 98:2001;2370-2374.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 2370-2374
    • Frauenfelder, H.1    McMahon, B.H.2    Austin, R.H.3    Chu, K.4    Groves, J.T.5
  • 3
    • 0029128015 scopus 로고
    • Functional linkage between the active site of alpha-lytic protease and distant regions of structure: Scanning alanine mutagenesis of a surface loop affects activity and substrate specificity
    • Mace J.E., Wilk B.J., Agard D.A. Functional linkage between the active site of alpha-lytic protease and distant regions of structure: scanning alanine mutagenesis of a surface loop affects activity and substrate specificity. J. Mol. Biol. 251:1995;116-134.
    • (1995) J. Mol. Biol. , vol.251 , pp. 116-134
    • MacE, J.E.1    Wilk, B.J.2    Agard, D.A.3
  • 4
    • 0033588178 scopus 로고    scopus 로고
    • Non-active site changes elicit broad-based cross-resistance of the HIV-1 protease to inhibitors
    • Olsen D.B., Stahlhut H.W., Rutkowski C.A., Schock H.B., van Olden A.L., Kuo L.C. Non-active site changes elicit broad-based cross-resistance of the HIV-1 protease to inhibitors. J. Biol. Chem. 274:1999;23699-23701.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23699-23701
    • Olsen, D.B.1    Stahlhut, H.W.2    Rutkowski, C.A.3    Schock, H.B.4    Van Olden, A.L.5    Kuo, L.C.6
  • 5
    • 0024374823 scopus 로고
    • Effects of distal point-site mutations on the binding and catalysis of dihydrofolate-reductase from Escherichia coli
    • Adams J., Johnson K., Matthews R., Benkovic S.J. Effects of distal point-site mutations on the binding and catalysis of dihydrofolate-reductase from Escherichia coli. Biochemistry. 28:1989;6611-6618.
    • (1989) Biochemistry , vol.28 , pp. 6611-6618
    • Adams, J.1    Johnson, K.2    Matthews, R.3    Benkovic, S.J.4
  • 6
    • 0037159205 scopus 로고    scopus 로고
    • Coupling interactions of distal residues enhance dihydrofolate reductase catalysis: Mutational effects on hydride transfer rates
    • Rajagopalan P.T.R., Lutz S., Benkovic S.J. Coupling interactions of distal residues enhance dihydrofolate reductase catalysis: mutational effects on hydride transfer rates. Biochemistry. 41:2002;12618-12628.
    • (2002) Biochemistry , vol.41 , pp. 12618-12628
    • Rajagopalan, P.T.R.1    Lutz, S.2    Benkovic, S.J.3
  • 7
    • 0038810233 scopus 로고    scopus 로고
    • Correlated motion and the effect of distal mutations in dihydrofolate reductase
    • Rod T.H., Radkiewicz J.L., Brooks C.L. III. Correlated motion and the effect of distal mutations in dihydrofolate reductase. Proc. Natl Acad. Sci. USA. 100:2003;6980-6985.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6980-6985
    • Rod, T.H.1    Radkiewicz, J.L.2    Brooks III, C.L.3
  • 8
    • 0037077656 scopus 로고    scopus 로고
    • Molecular dynamics at the root of expansion of function in the M69L inhibitor-resistant TEM beta-lactamase from Escherichia coli
    • Meroueh S.O., Roblin P., Golemi D., Mavegraud L., Vakulenko S.B., Zhang Y., et al. Molecular dynamics at the root of expansion of function in the M69L inhibitor-resistant TEM beta-lactamase from Escherichia coli. J. Am. Chem. Soc. 124:2002;9422-9430.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9422-9430
    • Meroueh, S.O.1    Roblin, P.2    Golemi, D.3    Mavegraud, L.4    Vakulenko, S.B.5    Zhang, Y.6
  • 9
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless S.W., Ranganathan R. Evolutionarily conserved pathways of energetic connectivity in protein families. Science. 286:1999;295-299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 10
    • 0021891887 scopus 로고
    • Effects of site-specific amino-acid modification on protein interactions and biological function
    • Ackers G.K., Smith F.R. Effects of site-specific amino-acid modification on protein interactions and biological function. Annu. Rev. Biochem. 54:1985;597-629.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 597-629
    • Ackers, G.K.1    Smith, F.R.2
  • 11
    • 0030322783 scopus 로고    scopus 로고
    • Double-mutant cycles: A powerful tool for analyzing protein structure and function
    • Horovitz A. Double-mutant cycles: a powerful tool for analyzing protein structure and function. Fold. Des. 1:1996;R121-R126.
    • (1996) Fold. Des. , vol.1
    • Horovitz, A.1
  • 12
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in protein
    • Süel G.M., Lockless S.W., Wall M.A., Ranganathan R. Evolutionarily conserved networks of residues mediate allosteric communication in protein. Nature Struct. Biol. 10:2003;59-69.
    • (2003) Nature Struct. Biol. , vol.10 , pp. 59-69
    • Süel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 13
    • 0034740693 scopus 로고    scopus 로고
    • Mechanism and role of PDZ domains in signaling complex assembly
    • Harris B.Z., Lim W.A. Mechanism and role of PDZ domains in signaling complex assembly. J. Cell Sci. 114:2001;3219-3231.
    • (2001) J. Cell Sci. , vol.114 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 14
    • 0037155199 scopus 로고    scopus 로고
    • PDZ domains: Structural modules for protein complex assembly
    • Hung A.Y., Sheng M. PDZ domains: structural modules for protein complex assembly. J. Biol. Chem. 277:2002;5699-5702.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5699-5702
    • Hung, A.Y.1    Sheng, M.2
  • 15
    • 0036876382 scopus 로고    scopus 로고
    • Signaling complex organization by PDZ domain proteins
    • Fan J.S., Zhang M. Signaling complex organization by PDZ domain proteins. Neurosignals. 11:2002;315-321.
    • (2002) Neurosignals , vol.11 , pp. 315-321
    • Fan, J.S.1    Zhang, M.2
  • 16
    • 0033617473 scopus 로고    scopus 로고
    • Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex
    • Hillier B.J., Christopherson K.S., Prehoda K.E., Bredt D.S., Lim W.A. Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex. Science. 284:1999;812-815.
    • (1999) Science , vol.284 , pp. 812-815
    • Hillier, B.J.1    Christopherson, K.S.2    Prehoda, K.E.3    Bredt, D.S.4    Lim, W.A.5
  • 17
    • 0037174873 scopus 로고    scopus 로고
    • PDZ7 of glutamate receptor interacting protein binds to its target via a novel hydrophobic surface area
    • Feng W., Fan J.S., Jiang M., Shi Y.W., Zhang M. PDZ7 of glutamate receptor interacting protein binds to its target via a novel hydrophobic surface area. J. Biol. Chem. 277:2002;41140-41146.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41140-41146
    • Feng, W.1    Fan, J.S.2    Jiang, M.3    Shi, Y.W.4    Zhang, M.5
  • 18
    • 0037416217 scopus 로고    scopus 로고
    • Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein Par6
    • Garrard S.M., Capaldo C.T., Gao L., Rosen M.K., Macara I.G., Tomchick D.R. Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein Par6. EMBO J. 22:2003;1125-1133.
    • (2003) EMBO J. , vol.22 , pp. 1125-1133
    • Garrard, S.M.1    Capaldo, C.T.2    Gao, L.3    Rosen, M.K.4    MacAra, I.G.5    Tomchick, D.R.6
  • 19
    • 0037319350 scopus 로고    scopus 로고
    • Direct interaction of two polarity complexes implicated in epithelial tight junction assembly
    • Hurd T.W., Gao L., Roh M.H., Macara I.G., Margolis B. Direct interaction of two polarity complexes implicated in epithelial tight junction assembly. Nature Cell Biol. 5:2003;137-142.
    • (2003) Nature Cell Biol. , vol.5 , pp. 137-142
    • Hurd, T.W.1    Gao, L.2    Roh, M.H.3    MacAra, I.G.4    Margolis, B.5
  • 20
    • 0029066512 scopus 로고
    • FAP-1: A protein tyrosine phosphatase that associates with Fas
    • Sato T., Irie S., Kitada S., Reed J.C. FAP-1: a protein tyrosine phosphatase that associates with Fas. Science. 268:1995;411-415.
    • (1995) Science , vol.268 , pp. 411-415
    • Sato, T.1    Irie, S.2    Kitada, S.3    Reed, J.C.4
  • 22
    • 12244288351 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in the regulation of cytokinesis
    • Herrmann L., Dittmar T., Erdmann K.S. The protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in the regulation of cytokinesis. Mol. Biol. Cell. 14:2003;230-240.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 230-240
    • Herrmann, L.1    Dittmar, T.2    Erdmann, K.S.3
  • 23
    • 0036241054 scopus 로고    scopus 로고
    • EphrinB phosphorylation and reverse signaling: Regulation by Src kinases and PTP-BL phosphatase
    • Palmer A., Zimmer M., Erdmann K.S., Eulenburg V., Porthin A., Heumann R., et al. EphrinB phosphorylation and reverse signaling: regulation by Src kinases and PTP-BL phosphatase. Mol. Cell. 9:2002;725-737.
    • (2002) Mol. Cell , vol.9 , pp. 725-737
    • Palmer, A.1    Zimmer, M.2    Erdmann, K.S.3    Eulenburg, V.4    Porthin, A.5    Heumann, R.6
  • 25
    • 0034646395 scopus 로고    scopus 로고
    • Solution structure of the PDZ2 domain from human phosphatase hPTP1E and its interactions with C-terminal peptides from the Fas receptors
    • Kozlov G., Gehring K., Ekiel I. Solution structure of the PDZ2 domain from human phosphatase hPTP1E and its interactions with C-terminal peptides from the Fas receptors. Biochemistry. 39:2000;2572-2580.
    • (2000) Biochemistry , vol.39 , pp. 2572-2580
    • Kozlov, G.1    Gehring, K.2    Ekiel, I.3
  • 26
    • 0036301446 scopus 로고    scopus 로고
    • Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the β2-β3 loop to PDZ domain-ligand interactions
    • Kozlov G., Banville D., Gehring K., Ekiel I. Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the β2-β3 loop to PDZ domain-ligand interactions. J. Mol. Biol. 320:2002;813-820.
    • (2002) J. Mol. Biol. , vol.320 , pp. 813-820
    • Kozlov, G.1    Banville, D.2    Gehring, K.3    Ekiel, I.4
  • 27
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle D.A., Lee A., Lewis J., Kim E., Sheng M., MacKinnon R. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell. 85:1996;1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 30
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari G., Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104:1982;4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 31
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • Lipari G., Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results. J. Am. Chem. Soc. 104:1982;4559-4570.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 32
    • 0030042698 scopus 로고    scopus 로고
    • Correlation between dynamics and high affinity binding in an SH2 domain interaction
    • Kay L.E., Muhandiram D.R., Farrow N.A., Aubin Y., Forman-Kay J.D. Correlation between dynamics and high affinity binding in an SH2 domain interaction. Biochemistry. 35:1996;361-368.
    • (1996) Biochemistry , vol.35 , pp. 361-368
    • Kay, L.E.1    Muhandiram, D.R.2    Farrow, N.A.3    Aubin, Y.4    Forman-Kay, J.D.5
  • 33
    • 0033988897 scopus 로고    scopus 로고
    • Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex
    • Lee A.L., Kinnear S.A., Wand A.J. Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex. Nature Struct. Biol. 7:2000;72-77.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 72-77
    • Lee, A.L.1    Kinnear, S.A.2    Wand, A.J.3
  • 34
    • 0034760077 scopus 로고    scopus 로고
    • Dynamic activation of protein function: A view emerging from NMR spectroscopy
    • Wand A.J. Dynamic activation of protein function: a view emerging from NMR spectroscopy. Nature Struct. Biol. 8:2001;926-931.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 926-931
    • Wand, A.J.1
  • 35
    • 0032991161 scopus 로고    scopus 로고
    • Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure
    • Mittermaier A., Kay L.E., Forman-Kay J.D. Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure. J. Biomol. NMR. 13:1999;181-185.
    • (1999) J. Biomol. NMR , vol.13 , pp. 181-185
    • Mittermaier, A.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 36
    • 0036385729 scopus 로고    scopus 로고
    • Side-chain dynamics of the SAP SH2 domain correlate with a binding hot spot and a region with conformational plasticity
    • Finerty P.J., Muhandiram R., Forman-Kay J.D. Side-chain dynamics of the SAP SH2 domain correlate with a binding hot spot and a region with conformational plasticity. J. Mol. Biol. 322:2002;605-620.
    • (2002) J. Mol. Biol. , vol.322 , pp. 605-620
    • Finerty, P.J.1    Muhandiram, R.2    Forman-Kay, J.D.3
  • 37
    • 0033620360 scopus 로고    scopus 로고
    • 13C NMR relaxation techniques for the study of protein methyl group dynamics in solution
    • 13C NMR relaxation techniques for the study of protein methyl group dynamics in solution. J. Am. Chem. Soc. 121:1999;2891-2902.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2891-2902
    • Lee, A.L.1    Flynn, P.F.2    Wand, A.J.3
  • 39
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel A.M., Akke M., Palmer A.G. III. Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol. Biol. 246:1995;144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer III, A.G.3
  • 40
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • Palmer A.G. III, Kroenke C.D., Loria J.P. Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol. 339:2001;204-238.
    • (2001) Methods Enzymol. , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 42
    • 0035901519 scopus 로고    scopus 로고
    • An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs
    • Loh A.P., Pawley N., Nicholson L.K., Oswald R.E. An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs. Biochemistry. 40:2001;4590-4600.
    • (2001) Biochemistry , vol.40 , pp. 4590-4600
    • Loh, A.P.1    Pawley, N.2    Nicholson, L.K.3    Oswald, R.E.4
  • 43
    • 0036721218 scopus 로고    scopus 로고
    • Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations
    • Kass I., Horovitz A. Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations. Proteins: Struct. Funct. Genet. 48:2002;611-617.
    • (2002) Proteins: Struct. Funct. Genet. , vol.48 , pp. 611-617
    • Kass, I.1    Horovitz, A.2
  • 44
    • 0037424515 scopus 로고    scopus 로고
    • Crystal structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class II PDZ target recognition and PDZ domain-mediated multimerization
    • Im Y.J., Park S.H., Rho S.H., Lee J.H., Kang G.B., Sheng M., et al. Crystal structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class II PDZ target recognition and PDZ domain-mediated multimerization. J. Biol. Chem. 278:2003;8501-8507.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8501-8507
    • Im, Y.J.1    Park, S.H.2    Rho, S.H.3    Lee, J.H.4    Kang, G.B.5    Sheng, M.6
  • 46
    • 0021658956 scopus 로고
    • Allostery without conformational change - A plausible model
    • Cooper A., Dryden D.T.F. Allostery without conformational change - a plausible model. Eur. Biophys. J. Biophys. Letters. 11:1984;103-109.
    • (1984) Eur. Biophys. J. Biophys. Letters , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.F.2
  • 48
    • 0031563812 scopus 로고    scopus 로고
    • Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation
    • Yang D., Mok Y.K., Forman-Kay J.D., Farrow N.A., Kay L.E. Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation. J. Mol. Biol. 272:1997;790-804.
    • (1997) J. Mol. Biol. , vol.272 , pp. 790-804
    • Yang, D.1    Mok, Y.K.2    Forman-Kay, J.D.3    Farrow, N.A.4    Kay, L.E.5
  • 49
    • 0037137214 scopus 로고    scopus 로고
    • Temperature dependence of the internal dynamics of a calmodulin-peptide complex
    • Lee A.L., Sharp K.A., Kranz J.K., Song X.J., Wand A.J. Temperature dependence of the internal dynamics of a calmodulin-peptide complex. Biochemistry. 41:2002;13814-13825.
    • (2002) Biochemistry , vol.41 , pp. 13814-13825
    • Lee, A.L.1    Sharp, K.A.2    Kranz, J.K.3    Song, X.J.4    Wand, A.J.5
  • 50
    • 0037457815 scopus 로고    scopus 로고
    • Dynamics and entropy of a calmodulin-peptide complex studied by NMR and molecular dynamics
    • Prabhu N.V., Lee A.L., Wand A.J., Sharp K.A. Dynamics and entropy of a calmodulin-peptide complex studied by NMR and molecular dynamics. Biochemistry. 42:2003;562-570.
    • (2003) Biochemistry , vol.42 , pp. 562-570
    • Prabhu, N.V.1    Lee, A.L.2    Wand, A.J.3    Sharp, K.A.4
  • 51
    • 0037222950 scopus 로고    scopus 로고
    • Cell polarity: Par6, aPKC and cytoskeletal crosstalk
    • Etienne-Manneville S., Hall A. Cell polarity: Par6, aPKC and cytoskeletal crosstalk. Curr. Opin. Cell Biol. 15:2003;67-72.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 67-72
    • Etienne-Manneville, S.1    Hall, A.2
  • 52
    • 0034253536 scopus 로고    scopus 로고
    • The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
    • Joberty G., Petersen C., Gao L., Macara I.G. The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nature Cell Biol. 2:2000;531-539.
    • (2000) Nature Cell Biol. , vol.2 , pp. 531-539
    • Joberty, G.1    Petersen, C.2    Gao, L.3    MacAra, I.G.4
  • 53
    • 0028026907 scopus 로고
    • A novel protein-tyrosine phosphatase with homology to both the cytoskeletal proteins of the band 4.1 family and junction-associated guanylate kinases
    • Banville D., Ahmad S., Stocco R., Shen S.H. A novel protein-tyrosine phosphatase with homology to both the cytoskeletal proteins of the band 4.1 family and junction-associated guanylate kinases. J. Biol. Chem. 269:1994;22320-22327.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22320-22327
    • Banville, D.1    Ahmad, S.2    Stocco, R.3    Shen, S.H.4
  • 54
    • 0032174747 scopus 로고    scopus 로고
    • Main-chain signal assignment for the PDZ2 domain from human protein tyrosine phosphatase hPTP1E and its complex with a C-terminal peptide from the Fas receptor
    • Ekiel I., Banville D., Shen S.H., Slon-Usakiewicz J.J., Koshy A., Gehring K. Main-chain signal assignment for the PDZ2 domain from human protein tyrosine phosphatase hPTP1E and its complex with a C-terminal peptide from the Fas receptor. J. Biomol. NMR. 12:1998;455-456.
    • (1998) J. Biomol. NMR , vol.12 , pp. 455-456
    • Ekiel, I.1    Banville, D.2    Shen, S.H.3    Slon-Usakiewicz, J.J.4    Koshy, A.5    Gehring, K.6
  • 56
    • 0029806697 scopus 로고    scopus 로고
    • Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy
    • Johnson P.E., Joshi M.D., Tomme P., Kilburn D.G., McIntosh L.P. Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy. Biochemistry. 35:1996;14381-14394.
    • (1996) Biochemistry , vol.35 , pp. 14381-14394
    • Johnson, P.E.1    Joshi, M.D.2    Tomme, P.3    Kilburn, D.G.4    McIntosh, L.P.5
  • 57
    • 0033029875 scopus 로고    scopus 로고
    • Assessing potential bias in the determination of rotational correlation times of proteins by NMR relaxation
    • Lee A.L., Wand A.J. Assessing potential bias in the determination of rotational correlation times of proteins by NMR relaxation. J. Biomol. NMR. 13:1999;101-112.
    • (1999) J. Biomol. NMR , vol.13 , pp. 101-112
    • Lee, A.L.1    Wand, A.J.2
  • 58
    • 0028674384 scopus 로고
    • Investigation of protein motions via relaxation measurements
    • Peng J.W., Wagner G. Investigation of protein motions via relaxation measurements. Methods Enzymol. 239:1994;563-596.
    • (1994) Methods Enzymol. , vol.239 , pp. 563-596
    • Peng, J.W.1    Wagner, G.2
  • 60
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.