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Volumn 7, Issue 12, 2012, Pages

Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis

Author keywords

[No Author keywords available]

Indexed keywords

ABP1P PROTEIN; ABPSH3 PROTEIN; FUNGAL PROTEIN; UNCLASSIFIED DRUG;

EID: 84871207088     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0051282     Document Type: Article
Times cited : (28)

References (43)
  • 1
    • 32344434479 scopus 로고    scopus 로고
    • The changing landscape of protein allostery
    • Swain JF, Gierasch LM, (2006) The changing landscape of protein allostery. Curr Opin Struct Biol 16: 102-108.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 102-108
    • Swain, J.F.1    Gierasch, L.M.2
  • 2
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman K, Kern D, (2007) Dynamic personalities of proteins. Nature 450: 964-972.
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 3
    • 33746363486 scopus 로고    scopus 로고
    • Domains, Motifs, and Scaffolds: The Role of Modular Interactions in the Evolution and Wiring of Cell Signaling Circuits
    • Bhattacharyya RP, Remenyi A, Yeh BJ, Lim WA, (2006) Domains, Motifs, and Scaffolds: The Role of Modular Interactions in the Evolution and Wiring of Cell Signaling Circuits. Annu Rev Biochem.
    • (2006) Annu Rev Biochem
    • Bhattacharyya, R.P.1    Remenyi, A.2    Yeh, B.J.3    Lim, W.A.4
  • 4
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • Lim WA, Richards FM, Fox RO, (1994) Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature 372: 375-379.
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 5
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrin- and actin-mediated endocytosis machinery
    • Kaksonen M, Toret CP, Drubin DG, (2005) A modular design for the clathrin- and actin-mediated endocytosis machinery. Cell 123: 305-320.
    • (2005) Cell , vol.123 , pp. 305-320
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 6
    • 0037085280 scopus 로고    scopus 로고
    • Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis
    • Fazi B, Cope MJ, Douangamath A, Ferracuti S, Schirwitz K, et al. (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.
    • (2002) J Biol Chem , vol.277 , pp. 5290-5298
    • Fazi, B.1    Cope, M.J.2    Douangamath, A.3    Ferracuti, S.4    Schirwitz, K.5
  • 7
    • 16244404272 scopus 로고    scopus 로고
    • The phosphoinositide phosphatase Sjl2 is recruited to cortical actin patches in the control of vesicle formation and fission during endocytosis
    • Stefan CJ, Padilla SM, Audhya A, Emr SD, (2005) The phosphoinositide phosphatase Sjl2 is recruited to cortical actin patches in the control of vesicle formation and fission during endocytosis. Mol Cell Biol 25: 2910-2923.
    • (2005) Mol Cell Biol , vol.25 , pp. 2910-2923
    • Stefan, C.J.1    Padilla, S.M.2    Audhya, A.3    Emr, S.D.4
  • 8
    • 70350351541 scopus 로고    scopus 로고
    • Structural, functional, and bioinformatic studies demonstrate the crucial role of an extended peptide binding site for the SH3 domain of yeast Abp1p
    • Stollar EJ, Garcia B, Chong PA, Rath A, Lin H, et al. (2009) Structural, functional, and bioinformatic studies demonstrate the crucial role of an extended peptide binding site for the SH3 domain of yeast Abp1p. J Biol Chem 284: 26918-26927.
    • (2009) J Biol Chem , vol.284 , pp. 26918-26927
    • Stollar, E.J.1    Garcia, B.2    Chong, P.A.3    Rath, A.4    Lin, H.5
  • 9
    • 40649118186 scopus 로고    scopus 로고
    • Recognition of non-canonical peptides by the yeast Fus1p SH3 domain: elucidation of a common mechanism for diverse SH3 domain specificities
    • Kim J, Lee CD, Rath A, Davidson AR, (2008) Recognition of non-canonical peptides by the yeast Fus1p SH3 domain: elucidation of a common mechanism for diverse SH3 domain specificities. J Mol Biol 377: 889-901.
    • (2008) J Mol Biol , vol.377 , pp. 889-901
    • Kim, J.1    Lee, C.D.2    Rath, A.3    Davidson, A.R.4
  • 10
    • 33846962112 scopus 로고    scopus 로고
    • Efficient T-cell receptor signaling requires a high-affinity interaction between the Gads C-SH3 domain and the SLP-76 RxxK motif
    • Seet BT, Berry DM, Maltzman JS, Shabason J, Raina M, et al. (2007) Efficient T-cell receptor signaling requires a high-affinity interaction between the Gads C-SH3 domain and the SLP-76 RxxK motif. Embo J 26: 678-689.
    • (2007) Embo J , vol.26 , pp. 678-689
    • Seet, B.T.1    Berry, D.M.2    Maltzman, J.S.3    Shabason, J.4    Raina, M.5
  • 11
    • 0346555269 scopus 로고    scopus 로고
    • Optimization of specificity in a cellular protein interaction network by negative selection
    • Zarrinpar A, Park SH, Lim WA, (2003) Optimization of specificity in a cellular protein interaction network by negative selection. Nature 426: 676-680.
    • (2003) Nature , vol.426 , pp. 676-680
    • Zarrinpar, A.1    Park, S.H.2    Lim, W.A.3
  • 12
    • 44849141472 scopus 로고    scopus 로고
    • Internal dynamics control activation and activity of the autoinhibited Vav DH domain
    • Li P, Martins IR, Amarasinghe GK, Rosen MK, (2008) Internal dynamics control activation and activity of the autoinhibited Vav DH domain. Nat Struct Mol Biol 15: 613-618.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 613-618
    • Li, P.1    Martins, I.R.2    Amarasinghe, G.K.3    Rosen, M.K.4
  • 13
    • 21744436606 scopus 로고    scopus 로고
    • Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region
    • Pufall MA, Lee GM, Nelson ML, Kang HS, Velyvis A, et al. (2005) Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region. Science 309: 142-145.
    • (2005) Science , vol.309 , pp. 142-145
    • Pufall, M.A.1    Lee, G.M.2    Nelson, M.L.3    Kang, H.S.4    Velyvis, A.5
  • 14
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single-domain signaling protein
    • Volkman BF, Lipson D, Wemmer DE, Kern D, (2001) Two-state allosteric behavior in a single-domain signaling protein. Science 291: 2429-2433.
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 15
    • 74549174000 scopus 로고    scopus 로고
    • Structural and energetic mechanisms of cooperative autoinhibition and activation of Vav1
    • Yu B, Martins IR, Li P, Amarasinghe GK, Umetani J, et al. (2010) Structural and energetic mechanisms of cooperative autoinhibition and activation of Vav1. Cell 140: 246-256.
    • (2010) Cell , vol.140 , pp. 246-256
    • Yu, B.1    Martins, I.R.2    Li, P.3    Amarasinghe, G.K.4    Umetani, J.5
  • 16
    • 64149129422 scopus 로고    scopus 로고
    • Regulation of C-type lectin antimicrobial activity by a flexible N-terminal prosegment
    • Mukherjee S, Partch CL, Lehotzky RE, Whitham CV, Chu H, et al. (2009) Regulation of C-type lectin antimicrobial activity by a flexible N-terminal prosegment. J Biol Chem 284: 4881-4888.
    • (2009) J Biol Chem , vol.284 , pp. 4881-4888
    • Mukherjee, S.1    Partch, C.L.2    Lehotzky, R.E.3    Whitham, C.V.4    Chu, H.5
  • 17
    • 0037995501 scopus 로고    scopus 로고
    • Structure and energetics of an allele-specific genetic interaction between dnaJ and dnaK: correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK
    • Landry SJ, (2003) Structure and energetics of an allele-specific genetic interaction between dnaJ and dnaK: correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK. Biochemistry 42: 4926-4936.
    • (2003) Biochemistry , vol.42 , pp. 4926-4936
    • Landry, S.J.1
  • 18
    • 51249097829 scopus 로고    scopus 로고
    • The affinity of Ets-1 for DNA is modulated by phosphorylation through transient interactions of an unstructured region
    • Lee GM, Pufall MA, Meeker CA, Kang HS, Graves BJ, et al. (2008) The affinity of Ets-1 for DNA is modulated by phosphorylation through transient interactions of an unstructured region. J Mol Biol 382: 1014-1030.
    • (2008) J Mol Biol , vol.382 , pp. 1014-1030
    • Lee, G.M.1    Pufall, M.A.2    Meeker, C.A.3    Kang, H.S.4    Graves, B.J.5
  • 19
    • 0031576335 scopus 로고    scopus 로고
    • Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: evidence for an activating surface
    • Nohaile M, Kern D, Wemmer D, Stedman K, Kustu S, (1997) Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: evidence for an activating surface. J Mol Biol 273: 299-316.
    • (1997) J Mol Biol , vol.273 , pp. 299-316
    • Nohaile, M.1    Kern, D.2    Wemmer, D.3    Stedman, K.4    Kustu, S.5
  • 20
    • 80052026932 scopus 로고    scopus 로고
    • cAMP-dependent protein kinase A selects the excited state of the membrane substrate phospholamban
    • Masterson LR, Yu T, Shi L, Wang Y, Gustavsson M, et al. (2011) cAMP-dependent protein kinase A selects the excited state of the membrane substrate phospholamban. J Mol Biol 412: 155-164.
    • (2011) J Mol Biol , vol.412 , pp. 155-164
    • Masterson, L.R.1    Yu, T.2    Shi, L.3    Wang, Y.4    Gustavsson, M.5
  • 22
    • 79955558165 scopus 로고    scopus 로고
    • Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy
    • Masterson LR, Shi L, Metcalfe E, Gao J, Taylor SS, et al. (2011) Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy. Proc Natl Acad Sci U S A 108: 6969-6974.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 6969-6974
    • Masterson, L.R.1    Shi, L.2    Metcalfe, E.3    Gao, J.4    Taylor, S.S.5
  • 23
    • 34548548791 scopus 로고    scopus 로고
    • The biologically relevant targets and binding affinity requirements for the function of the yeast actin-binding protein 1 Src-homology 3 domain vary with genetic context
    • Haynes J, Garcia B, Stollar EJ, Rath A, Andrews BJ, et al. (2007) The biologically relevant targets and binding affinity requirements for the function of the yeast actin-binding protein 1 Src-homology 3 domain vary with genetic context. Genetics 176: 193-208.
    • (2007) Genetics , vol.176 , pp. 193-208
    • Haynes, J.1    Garcia, B.2    Stollar, E.J.3    Rath, A.4    Andrews, B.J.5
  • 24
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5
  • 25
    • 34249765651 scopus 로고
    • NMRView: a computer program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA, (1994) NMRView: a computer program for the visualization and analysis of NMR data. Journal of Biomolecular NMR 4: 603-614.
    • (1994) Journal of Biomolecular NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 26
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced hetero-nuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay LE, Keifer P, Saarinen T, (1992) Pure absorption gradient enhanced hetero-nuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114: 10663-10665.
    • (1992) J Am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 27
    • 0026890433 scopus 로고
    • Measurement of two-bond JCOH alpha coupling constants in proteins uniformly enriched with 13C
    • Vuister GW, Bax A, (1992) Measurement of two-bond JCOH alpha coupling constants in proteins uniformly enriched with 13C. J Biomol NMR 2: 401-405.
    • (1992) J Biomol NMR , vol.2 , pp. 401-405
    • Vuister, G.W.1    Bax, A.2
  • 28
    • 0028503463 scopus 로고
    • A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium
    • Farrow N, Zhang O, Forman-Kay JD, Kay LE, (1994) A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium. J Biomol NMR 4: 727-734.
    • (1994) J Biomol NMR , vol.4 , pp. 727-734
    • Farrow, N.1    Zhang, O.2    Forman-Kay, J.D.3    Kay, L.E.4
  • 30
    • 9444225935 scopus 로고    scopus 로고
    • Java Treeview-extensible visualization of microarray data
    • Saldanha AJ, (2004) Java Treeview-extensible visualization of microarray data. Bioinformatics 20: 3246-3248.
    • (2004) Bioinformatics , vol.20 , pp. 3246-3248
    • Saldanha, A.J.1
  • 31
    • 0028356365 scopus 로고
    • Exchange kinetics of individual amide protons in 15N-labeled helical peptides measured by isotope-edited NMR
    • Rohl CA, Baldwin RL, (1994) Exchange kinetics of individual amide protons in 15N-labeled helical peptides measured by isotope-edited NMR. Biochemistry 33: 7760-7767.
    • (1994) Biochemistry , vol.33 , pp. 7760-7767
    • Rohl, C.A.1    Baldwin, R.L.2
  • 33
    • 39649098037 scopus 로고    scopus 로고
    • Analysis of the thermodynamics of binding of an SH3 domain to proline-rich peptides using a chimeric fusion protein
    • Candel AM, van Nuland NA, Martin-Sierra FM, Martinez JC, Conejero-Lara F, (2008) Analysis of the thermodynamics of binding of an SH3 domain to proline-rich peptides using a chimeric fusion protein. J Mol Biol 377: 117-135.
    • (2008) J Mol Biol , vol.377 , pp. 117-135
    • Candel, A.M.1    van Nuland, N.A.2    Martin-Sierra, F.M.3    Martinez, J.C.4    Conejero-Lara, F.5
  • 34
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant JM, (1977) Heat capacity and entropy changes in processes involving proteins. Proc Natl Acad Sci U S A 74: 2236-2240.
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 35
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar RS, Record MT Jr, (1994) Coupling of local folding to site-specific binding of proteins to DNA. Science 263: 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 36
    • 0030736323 scopus 로고    scopus 로고
    • Protein-DNA recognition complexes: conservation of structure and binding energy in the transition state
    • Jen-Jacobson L, (1997) Protein-DNA recognition complexes: conservation of structure and binding energy in the transition state. Biopolymers 44: 153-180.
    • (1997) Biopolymers , vol.44 , pp. 153-180
    • Jen-Jacobson, L.1
  • 37
    • 6344219895 scopus 로고    scopus 로고
    • Is allostery an intrinsic property of all dynamic proteins?
    • Gunasekaran K, Ma B, Nussinov R, (2004) Is allostery an intrinsic property of all dynamic proteins? Proteins 57: 433-443.
    • (2004) Proteins , vol.57 , pp. 433-443
    • Gunasekaran, K.1    Ma, B.2    Nussinov, R.3
  • 38
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson T, Nash P, (2003) Assembly of cell regulatory systems through protein interaction domains. Science 300: 445-452.
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 39
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • James LC, Roversi P, Tawfik DS, (2003) Antibody multispecificity mediated by conformational diversity. Science 299: 1362-1367.
    • (2003) Science , vol.299 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2    Tawfik, D.S.3
  • 40
    • 0034283147 scopus 로고    scopus 로고
    • Specificity in protein-protein interactions: the structural basis for dual recognition in endonuclease colicin-immunity protein complexes
    • Kuhlmann UC, Pommer AJ, Moore GR, James R, Kleanthous C, (2000) Specificity in protein-protein interactions: the structural basis for dual recognition in endonuclease colicin-immunity protein complexes. J Mol Biol 301: 1163-1178.
    • (2000) J Mol Biol , vol.301 , pp. 1163-1178
    • Kuhlmann, U.C.1    Pommer, A.J.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 41
    • 0036682133 scopus 로고    scopus 로고
    • Two-step binding mechanism for T-cell receptor recognition of peptide MHC
    • Wu LC, Tuot DS, Lyons DS, Garcia KC, Davis MM, (2002) Two-step binding mechanism for T-cell receptor recognition of peptide MHC. Nature 418: 552-556.
    • (2002) Nature , vol.418 , pp. 552-556
    • Wu, L.C.1    Tuot, D.S.2    Lyons, D.S.3    Garcia, K.C.4    Davis, M.M.5
  • 42
    • 70350348011 scopus 로고    scopus 로고
    • NMR spectroscopy brings invisible protein states into focus
    • Baldwin AJ, Kay LE, (2009) NMR spectroscopy brings invisible protein states into focus. Nat Chem Biol 5: 808-814.
    • (2009) Nat Chem Biol , vol.5 , pp. 808-814
    • Baldwin, A.J.1    Kay, L.E.2
  • 43
    • 70349093561 scopus 로고    scopus 로고
    • Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes
    • Clore GM, Iwahara J, (2009) Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes. Chem Rev 109: 4108-4139.
    • (2009) Chem Rev , vol.109 , pp. 4108-4139
    • Clore, G.M.1    Iwahara, J.2


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