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Volumn 3, Issue , 2013, Pages

The transition state structure for coupled binding and folding of disordered protein domains

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; PROTEIN BINDING;

EID: 84883780574     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep02076     Document Type: Article
Times cited : (81)

References (46)
  • 2
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Wright, P. E. & Dyson, H. J. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6, 197-208 (2005).
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 197-208
    • Wright, P.E.1    Dyson, H.J.2
  • 3
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. Intrinsically unstructured proteins. Trends Biochem. Sci. 27, 527-533 (2002).
    • (2002) Trends Biochem. Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 4
    • 33744961763 scopus 로고    scopus 로고
    • Intrinsic disorder in transcription factors
    • Liu, J. et al. Intrinsic disorder in transcription factors. Biochemistry 45, 6873-6888 (2006).
    • (2006) Biochemistry , vol.45 , pp. 6873-6888
    • Liu, J.1
  • 5
    • 80055012207 scopus 로고    scopus 로고
    • Expanding the proteome: Disordered and alternatively folded proteins
    • Dyson, H. J. Expanding the proteome: disordered and alternatively folded proteins. Q. Rev. Biophys., 1-52 (2011).
    • (2011) Q. Rev. Biophys , pp. 1-52
    • Dyson, H.J.1
  • 6
    • 34547943482 scopus 로고    scopus 로고
    • Molecular principles of the interactions of disordered proteins
    • Meszaros, B., Tompa, P., Simon, I. & Dosztanyi, Z. Molecular principles of the interactions of disordered proteins. J. Mol. Biol. 372, 549-561 (2007).
    • (2007) J. Mol. Biol , vol.372 , pp. 549-561
    • Meszaros, B.1    Tompa, P.2    Simon, I.3    Dosztanyi, Z.4
  • 8
    • 0037203771 scopus 로고    scopus 로고
    • Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators
    • Demarest, S. J. et al. Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. Nature 415, 549-553 (2002).
    • (2002) Nature , vol.415 , pp. 549-553
    • Demarest, S.J.1
  • 9
    • 33744960022 scopus 로고    scopus 로고
    • Structural diversity in p160/CREB-binding protein coactivator complexes
    • Waters, L. et al. Structural diversity in p160/CREB-binding protein coactivator complexes. J. Biol. Chem. 281, 14787-14795 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 14787-14795
    • Waters, L.1
  • 10
    • 24344487414 scopus 로고    scopus 로고
    • Crystal structure of IRF-3 in complex with CBP
    • Qin, B. Y. et al. Crystal structure of IRF-3 in complex with CBP. Structure 13, 1269-1277 (2005).
    • (2005) Structure , vol.13 , pp. 1269-1277
    • Qin, B.Y.1
  • 11
    • 78649284498 scopus 로고    scopus 로고
    • Structure of the p53 transactivation domain in complex with the nuclear receptor coactivator binding domain of CREB binding protein
    • Lee, C. W., Martinez-Yamout, M. A., Dyson, H. J. &Wright, P. E. Structure of the p53 transactivation domain in complex with the nuclear receptor coactivator binding domain of CREB binding protein. Biochemistry 49, 9964-9971 (2010).
    • (2011) Biochemistry , vol.49 , pp. 9964-9971
    • Lee, C.W.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 12
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen, H. et al. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90, 569-580 (1997).
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1
  • 13
    • 0034234237 scopus 로고    scopus 로고
    • CBP/p300 in cell growth, transformation, and development
    • Goodman, R. H. & Smolik, S. CBP/p300 in cell growth, transformation, and development. Genes Dev. 14, 1553-1577 (2000).
    • (2000) Genes Dev , vol.14 , pp. 1553-1577
    • Goodman, R.H.1    Smolik, S.2
  • 14
    • 77955442470 scopus 로고    scopus 로고
    • Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP
    • Kjaergaard, M., Teilum, K. & Poulsen, F. M. Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. Proc. Natl. Acad. Sci. USA 107, 12535-12540 (2010).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12535-12540
    • Kjaergaard, M.1    Teilum, K.2    Poulsen, F.M.3
  • 15
    • 38849144628 scopus 로고    scopus 로고
    • NMR relaxation study of the complex formed between CBP and the activation domain of the nuclear hormone receptor coactivator ACTR
    • Ebert, M. O., Bae, S. H., Dyson, H. J. &Wright, P. E. NMR relaxation study of the complex formed between CBP and the activation domain of the nuclear hormone receptor coactivator ACTR. Biochemistry 47, 1299-1308 (2008).
    • (2008) Biochemistry , vol.47 , pp. 1299-1308
    • Ebert, M.O.1    Bae, S.H.2    Dyson, H.J.3    Wright, P.E.4
  • 16
    • 77955099224 scopus 로고    scopus 로고
    • Temperature-dependent structural changes in intrinsically disordered proteins: Formation of alpha-helices or loss of polyproline II?
    • Kjaergaard, M. et al. Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II? Protein Sci. 19, 1555-1564 (2010).
    • (2011) Protein Sci , vol.19 , pp. 1555-1564
    • Kjaergaard, M.1
  • 17
    • 84867280715 scopus 로고    scopus 로고
    • Fast association and slow transitions in the interaction between two intrinsically disordered protein domains
    • Dogan, J., Schmidt, T., Mu, X., Engstro, A?&Jemth, P. Fast Association and Slow Transitions in the Interaction between Two Intrinsically Disordered Protein Domains. J. Biol. Chem. 287, 34316-34324 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 34316-34324
    • Dogan, J.1    Schmidt, T.2    Mu, X.3    Engstro, A.4    Jemth, P.5
  • 18
    • 84859396047 scopus 로고    scopus 로고
    • Is a malleable protein necessarily highly dynamic? the hydrophobic core of the nuclear coactivator binding domain is well ordered
    • Kjaergaard, M., Poulsen, F. M. & Teilum, K. Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered. Biophys. J. 102, 1627-1635 (2012).
    • (2012) Biophys. J , vol.102 , pp. 1627-1635
    • Kjaergaard, M.1    Poulsen, F.M.2    Teilum, K.3
  • 19
    • 0346733326 scopus 로고    scopus 로고
    • Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB-binding protein
    • Demarest, S. J., Deechongkit, S., Dyson, H. J., Evans, R. M.&Wright, P. E. Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB-binding protein. Protein Sci. 13, 203-210 (2004).
    • (2004) Protein Sci , vol.13 , pp. 203-210
    • Demarest, S.J.1    Deechongkit, S.2    Dyson, H.J.3    Evans, R.M.4    Wright, P.E.5
  • 20
    • 2542599277 scopus 로고    scopus 로고
    • Phi-value analysis and the nature of protein-folding transition states
    • Fersht, A. R. & Sato, S. Phi-value analysis and the nature of protein-folding transition states. Proc. Natl. Acad. Sci. USA 101, 7976-7981 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7976-7981
    • Fersht, A.R.1    Sato, S.2
  • 21
    • 65249099497 scopus 로고    scopus 로고
    • Fundamental aspects of protein-protein association kinetics
    • Schreiber, G., Haran, G. & Zhou, H. X. Fundamental aspects of protein-protein association kinetics. Chem. Rev. 109, 839-860 (2009).
    • (2009) Chem. Rev , vol.109 , pp. 839-860
    • Schreiber, G.1    Haran, G.2    Zhou, H.X.3
  • 22
    • 0032570873 scopus 로고    scopus 로고
    • Forcing thermodynamically unfolded proteins to fold
    • Baskakov, I.&Bolen, D. W. Forcing thermodynamically unfolded proteins to fold. J. Biol. Chem. 273, 4831-4834 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 4831-4834
    • Baskakov, I.1    Bolen, D.W.2
  • 23
    • 0032518944 scopus 로고    scopus 로고
    • The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and-independent pathways
    • Voegel, J. J. et al. The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and-independent pathways. EMBO J. 17, 507-519 (1998).
    • (1998) EMBO J , vol.17 , pp. 507-519
    • Voegel, J.J.1
  • 24
    • 1842740359 scopus 로고    scopus 로고
    • A Conserved alpha-helical motif mediates the binding of diverse nuclear proteins to the SRC1 interaction domain of CBP
    • Matsuda, S. et al. A Conserved alpha-helical motif mediates the binding of diverse nuclear proteins to the SRC1 interaction domain of CBP. J. Biol. Chem. 279, 14055-14064 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 14055-14064
    • Matsuda, S.1
  • 25
    • 33749679602 scopus 로고    scopus 로고
    • Functional interaction of CREB binding protein (CBP) with nuclear transport proteins and modulation by HDAC inhibitors
    • Ryan, C. M., Harries, J. C., Kindle, K. B., Collins, H. M. & Heery, D. M. Functional interaction of CREB binding protein (CBP) with nuclear transport proteins and modulation by HDAC inhibitors. Cell cycle 5, 2146-2152 (2006).
    • (2006) Cell Cycle , vol.5 , pp. 2146-2152
    • Ryan, C.M.1    Harries, J.C.2    Kindle, K.B.3    Collins, H.M.4    Heery, D.M.5
  • 26
    • 0031694146 scopus 로고    scopus 로고
    • Kinetic epitope mapping of the chicken lysozyme HyHEL-10 Fab complex: Delineation of docking trajectories
    • Taylor, M. G., Rajpal, A. & Kirsch, J. F. Kinetic epitope mapping of the chicken lysozyme. HyHEL-10 Fab complex: delineation of docking trajectories. Protein Sci. 7, 1857-1867 (1998).
    • (1998) Protein Sci , vol.7 , pp. 1857-1867
    • Taylor, M.G.1    Rajpal, A.2    Kirsch, J.F.3
  • 27
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • Sugase, K., Dyson, H. J.&Wright, P. E. Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 447, 1021-1026 (2007).
    • (2007) Nature , vol.447 , pp. 1021-1026
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 28
    • 42949161558 scopus 로고    scopus 로고
    • Binding-induced folding of a natively unstructured transcription factor
    • Turjanski, A. G., Gutkind, J. S., Best, R. B. &Hummer, G. Binding-induced folding of a natively unstructured transcription factor. PLoS Comp. Biol. 4, e1000060 (2008).
    • (2008) PLoS Comp. Biol , vol.4 , pp. e1000060
    • Turjanski, A.G.1    Gutkind, J.S.2    Best, R.B.3    Hummer, G.4
  • 29
    • 84855656923 scopus 로고    scopus 로고
    • Side-chain interactions form late and cooperatively in the binding reaction between disordered peptides and PDZ domains
    • Haq, S. R. et al. Side-chain interactions form late and cooperatively in the binding reaction between disordered peptides and PDZ domains. J. Am. Chem. Soc. 134, 599-605 (2012).
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 599-605
    • Haq, S.R.1
  • 30
    • 84857653889 scopus 로고    scopus 로고
    • The transition state of coupled folding and binding for a flexible beta-finger
    • Karlsson, O. A., Chi, C. N., Engstro, A? & Jemth, P. The transition state of coupled folding and binding for a flexible beta-finger. J. Mol. Biol. 417, 253-261 (2012).
    • (2012) J. Mol. Biol , vol.417 , pp. 253-261
    • Karlsson, O.A.1    Chi, C.N.2    Engstro, A.3    Jemth, P.4
  • 31
    • 79952741171 scopus 로고    scopus 로고
    • Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction
    • Bachmann, A., Wildemann, D., Praetorius, F., Fischer, G. & Kiefhaber, T. Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction. Proc. Natl. Acad. Sci. USA 108, 3952-3957 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 3952-3957
    • Bachmann, A.1    Wildemann, D.2    Praetorius, F.3    Fischer, G.4    Kiefhaber, T.5
  • 32
    • 84869218677 scopus 로고    scopus 로고
    • A folding-After-binding mechanism describes the recognition between the transactivation domain of c-Myb and the KIX domain of the CREB-binding protein
    • Gianni, S., Morrone, A., Giri, R. & Brunori, M. A folding-After-binding mechanism describes the recognition between the transactivation domain of c-Myb and the KIX domain of the CREB-binding protein. Biochem. Biophys. Res. Commun. 428, 205-209 (2012).
    • (2012) Biochem Biophys. Res. Commun , vol.428 , pp. 205-209
    • Gianni, S.1    Morrone, A.2    Giri, R.3    Brunori, M.4
  • 33
    • 84874963976 scopus 로고    scopus 로고
    • A folded excited state of ligand-free nuclear coactivator binding domain (NCBD) Underlies Plasticity in Ligand Recognition
    • In press
    • Kjaergaard, M., Andersen, L., Nielsen, L. D.&lTeilum, K.AFolded Excited State of Ligand-Free Nuclear Coactivator Binding Domain (NCBD) Underlies Plasticity in Ligand Recognition. Biochemistry In press, doi:10.1021/bi4001062 (2013).
    • (2013) Biochemistry
    • Kjaergaard, M.1    Andersen, L.2    Nielsen, L.D.3    Teilum, K.4
  • 34
    • 84874086468 scopus 로고    scopus 로고
    • Single-molecule studies of intrinsically disordered proteins using solid-state nanopores
    • Japrung, D. et al. Single-molecule studies of intrinsically disordered proteins using solid-state nanopores. Anal. Chem. 85, 2449-2456 (2013).
    • (2013) Anal. Chem , vol.85 , pp. 2449-2456
    • Japrung, D.1
  • 35
    • 69549120472 scopus 로고    scopus 로고
    • Conformational selection or induced fit: A flux description of reaction mechanism
    • Hammes, G. G., Chang, Y. C. & Oas, T. G. Conformational selection or induced fit: A flux description of reaction mechanism. Proc. Natl. Acad. Sci. U S A 106, 13737-13741 (2009).
    • (2009) Proc. Natl. Acad. Sci. U S A , vol.106 , pp. 13737-13741
    • Hammes, G.G.1    Chang, Y.C.2    Oas, T.G.3
  • 36
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 254, 260-288 (1995).
    • (1995) J. Mol. Biol , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 37
    • 13244295627 scopus 로고    scopus 로고
    • The LxxLL motif: A multifunctional binding sequence in transcriptional regulation
    • Plevin, M. J., Mills, M.M. & Ikura, M. The LxxLL motif: A multifunctional binding sequence in transcriptional regulation. Trends Biochem. Sci. 30, 66-69 (2005).
    • (2005) Trends Biochem. Sci , vol.30 , pp. 66-69
    • Plevin, M.J.1    Mills, M.M.2    Ikura, M.3
  • 38
    • 84864581257 scopus 로고    scopus 로고
    • A preformed binding interface in the unbound ensemble of an intrinsically disordered protein: Evidence from molecular simulations
    • Knott, M. &Best, R. B. A preformed binding interface in the unbound ensemble of an intrinsically disordered protein: evidence from molecular simulations. PLoS Comp. Biol. 8, e1002605 (2012).
    • (2012) PLoS Comp. Biol , vol.8 , pp. e1002605
    • Knott, M.1    Best, R.B.2
  • 39
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter, M., Simon, I., Friedrich, P. & Tompa, P. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J. Mol. Biol. 338, 1015-1026 (2004).
    • (2004) J. Mol. Biol , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 40
    • 27144528728 scopus 로고    scopus 로고
    • Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation
    • Sivakolundu, S. G., Bashford, D. & Kriwacki, R.W. Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation. J. Mol. Biol. 353, 1118-1128 (2005).
    • (2005) J. Mol. Biol , vol.353 , pp. 1118-1128
    • Sivakolundu, S.G.1    Bashford, D.2    Kriwacki, R.W.3
  • 41
    • 84859224210 scopus 로고    scopus 로고
    • Microsecond molecular dynamics simulations of intrinsically disordered proteins involved in the oxidative stress response
    • Cino, E. A., Wong-ekkabut, J., Karttunen, M. & Choy, W. Y. Microsecond molecular dynamics simulations of intrinsically disordered proteins involved in the oxidative stress response. PLOS ONE 6, e27371 (2011).
    • (2011) PLOS ONE , vol.6 , pp. e27371
    • Cino, E.A.1    Wong-Ekkabut, J.2    Karttunen, M.3    Choy, W.Y.4
  • 42
    • 26944450513 scopus 로고    scopus 로고
    • An electrostatic steering mechanism of Cdc42 recognition by Wiskott-Aldrich syndrome proteins
    • Hemsath, L., Dvorsky, R., Fiegen, D., Carlier, M. F. & Ahmadian, M. R. An electrostatic steering mechanism of Cdc42 recognition by Wiskott-Aldrich syndrome proteins. Mol. Cell 20, 313-324 (2005).
    • (2005) Mol. Cell , vol.20 , pp. 313-324
    • Hemsath, L.1    Dvorsky, R.2    Fiegen, D.3    Carlier, M.F.4    Ahmadian, M.R.5
  • 43
    • 0033923367 scopus 로고    scopus 로고
    • Rational design of faster associating and tighter binding protein complexes
    • Selzer, T., Albeck, S. & Schreiber, G. Rational design of faster associating and tighter binding protein complexes. Nat. Struct. Biol. 7, 537-541 (2000).
    • (2000) Nat. Struct. Biol , vol.7 , pp. 537-541
    • Selzer, T.1    Albeck, S.2    Schreiber, G.3
  • 44
    • 3042594710 scopus 로고    scopus 로고
    • Electrostatically optimized Ras-binding Ral guanine dissociation stimulator mutants increase the rate of association by stabilizing the encounter complex
    • Kiel, C., Selzer, T., Shaul, Y., Schreiber, G. & Herrmann, C. Electrostatically optimized Ras-binding Ral guanine dissociation stimulator mutants increase the rate of association by stabilizing the encounter complex. Proc. Natl. Acad. Sci. USA 101, 9223-9228 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9223-9228
    • Kiel, C.1    Selzer, T.2    Shaul, Y.3    Schreiber, G.4    Herrmann, C.5
  • 45
    • 73249133356 scopus 로고    scopus 로고
    • Direct observation of ultrafast folding and denatured state dynamics in single protein molecules
    • Neuweiler, H., Johnson, C. M. & Fersht, A. R. Direct observation of ultrafast folding and denatured state dynamics in single protein molecules. Proc. Natl. Acad. Sci. USA 106, 18569-18574 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 18569-18574
    • Neuweiler, H.1    Johnson, C.M.2    Fersht, A.R.3
  • 46
    • 21844437963 scopus 로고    scopus 로고
    • The study of bimolecular reactions under non-pseudo-first order conditions
    • Malatesta, F. The study of bimolecular reactions under non-pseudo-first order conditions. Biophys. Chem. 116, 251-256 (2005).
    • (2005) Biophys. Chem , vol.116 , pp. 251-256
    • Malatesta, F.1


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