메뉴 건너뛰기




Volumn 448, Issue 7151, 2007, Pages 325-329

Conformational entropy in molecular recognition by proteins

Author keywords

[No Author keywords available]

Indexed keywords

CALMODULIN; LIGAND; PROTEIN;

EID: 34447503697     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05959     Document Type: Article
Times cited : (573)

References (34)
  • 1
    • 0036424666 scopus 로고    scopus 로고
    • Structural basis of macromolecular recognition
    • Wodak, S. J. & Janin, J. Structural basis of macromolecular recognition. Adv. Prot. Chem. 61, 9-73 (2002).
    • (2002) Adv. Prot. Chem , vol.61 , pp. 9-73
    • Wodak, S.J.1    Janin, J.2
  • 2
    • 0028916599 scopus 로고    scopus 로고
    • Clackson, T. & Wells, J. A. A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386 (1995).
    • Clackson, T. & Wells, J. A. A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386 (1995).
  • 3
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R. S. & Record, M. T. Jr. Coupling of local folding to site-specific binding of proteins to DNA. Science 263, 777-784 (1994).
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 4
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant, J. M. Heat capacity and entropy changes in processes involving proteins. Proc. Natl Acad. Sci. USA 74, 2236-2240 (1977).
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 5
    • 0001666112 scopus 로고
    • Entropy changes accompanying association reactions of proteins
    • Steinberg, I. Z. & Scheraga, H. A. Entropy changes accompanying association reactions of proteins. J. Biol. Chem. 238, 172-181 (1963).
    • (1963) J. Biol. Chem , vol.238 , pp. 172-181
    • Steinberg, I.Z.1    Scheraga, H.A.2
  • 6
    • 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. Lett. 11, 103-109 (1984).
    • (1984) Eur. Biophys. J. Biophys. Lett , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.F.2
  • 7
    • 0023475026 scopus 로고
    • Configurational entropy of native proteins
    • Karplus, M., Ichiye, T. & Pettitt, B. M. Configurational entropy of native proteins. Biophys. J. 52, 1083-1085 (1987).
    • (1987) Biophys. J , vol.52 , pp. 1083-1085
    • Karplus, M.1    Ichiye, T.2    Pettitt, B.M.3
  • 8
    • 33645994825 scopus 로고    scopus 로고
    • Flexibility and conformational entropy in protein-protein binding
    • Grunberg, R., Nilges, M. & Leckner, J. Flexibility and conformational entropy in protein-protein binding. Structure 14, 683-693 (2006).
    • (2006) Structure , vol.14 , pp. 683-693
    • Grunberg, R.1    Nilges, M.2    Leckner, J.3
  • 9
    • 33646945580 scopus 로고    scopus 로고
    • Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution
    • Igumenova, T. I., Frederick, K. K. & Wand, A. J. Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution. Chem. Rev. 106, 1672-1699 (2006).
    • (2006) Chem. Rev , vol.106 , pp. 1672-1699
    • Igumenova, T.I.1    Frederick, K.K.2    Wand, A.J.3
  • 11
    • 0347949547 scopus 로고    scopus 로고
    • Regulation of cell cycle progression by calcium/calmodulin-dependent pathways
    • Kahl, C. R. & Means, A. R. Regulation of cell cycle progression by calcium/calmodulin-dependent pathways. Endocr. Rev. 24, 719-736 (2003).
    • (2003) Endocr. Rev , vol.24 , pp. 719-736
    • Kahl, C.R.1    Means, A.R.2
  • 12
    • 0003161862 scopus 로고    scopus 로고
    • Calmodulin target database
    • Yap, K. L. et al. Calmodulin target database. J. Struct. Funct. Genom. 1, 8-14 (2000).
    • (2000) J. Struct. Funct. Genom , vol.1 , pp. 8-14
    • Yap, K.L.1
  • 13
    • 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, 72-77 (2000).
    • (2000) Nature Struct. Biol , vol.7 , pp. 72-77
    • Lee, A.L.1    Kinnear, S.A.2    Wand, A.J.3
  • 14
    • 0022549779 scopus 로고
    • Calmodulin binding domains: Characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase
    • Lukas, T. J. et al. Calmodulin binding domains: characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase. Biochemistry 25, 1458-1464 (1986).
    • (1986) Biochemistry , vol.25 , pp. 1458-1464
    • Lukas, T.J.1
  • 15
    • 0027954427 scopus 로고
    • Characterization of the calmodulin-binding domain of rat cerebellar nitric oxide synthase
    • Zhang, M. & Vogel, H. J. Characterization of the calmodulin-binding domain of rat cerebellar nitric oxide synthase. J. Biol. Chem. 269, 981-985 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 981-985
    • Zhang, M.1    Vogel, H.J.2
  • 16
    • 0030714072 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase kinase: Identification of regulatory domains
    • Tokumitsu, H. et al. Calcium/calmodulin-dependent protein kinase kinase: identification of regulatory domains. Biochemistry 36, 12823-12827 (1997).
    • (1997) Biochemistry , vol.36 , pp. 12823-12827
    • Tokumitsu, H.1
  • 17
    • 0029871290 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I
    • Goldberg, J., Nairn, A. C. & Kuriyan, J. Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I. Cell 84, 875-887 (1996).
    • (1996) Cell , vol.84 , pp. 875-887
    • Goldberg, J.1    Nairn, A.C.2    Kuriyan, J.3
  • 18
    • 0025807931 scopus 로고
    • Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain
    • Charbonneau, H. et al. Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain. Biochemistry 30, 7931-7940 (1991).
    • (1991) Biochemistry , vol.30 , pp. 7931-7940
    • Charbonneau, H.1
  • 19
    • 0031567108 scopus 로고    scopus 로고
    • Energetics of target peptide recognition by calmodulin: A calorimetric study
    • Wintrode, P. L. & Privalov, P. L. Energetics of target peptide recognition by calmodulin: a calorimetric study. J. Mol. Biol. 266, 1050-1062 (1997).
    • (1997) J. Mol. Biol , vol.266 , pp. 1050-1062
    • Wintrode, P.L.1    Privalov, P.L.2
  • 20
    • 0035958004 scopus 로고    scopus 로고
    • Energetics of target peptide binding by calmodulin reveals different modes of binding
    • Brokx, R. D. et al. Energetics of target peptide binding by calmodulin reveals different modes of binding. J. Biol. Chem. 276, 14083-14091 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 14083-14091
    • Brokx, R.D.1
  • 21
    • 0028282555 scopus 로고
    • 15N NMR relaxation
    • 15N NMR relaxation. Biochemistry 33, 5984-6003 (1994).
    • (1994) Biochemistry , vol.33 , pp. 5984-6003
    • Farrow, N.A.1
  • 22
    • 0038037171 scopus 로고    scopus 로고
    • Temperature dependence of anisotropic protein backbone dynamics
    • Wang, T., Cai, S. & Zuiderweg, E. R. Temperature dependence of anisotropic protein backbone dynamics. J. Am. Chem. Soc. 125, 8639-8643 (2003).
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 8639-8643
    • Wang, T.1    Cai, S.2    Zuiderweg, E.R.3
  • 23
    • 0029176895 scopus 로고
    • Measurement of H-2 T-1 and T-1p relaxation-times in uniformly C-13-Labeled and fractionally H-2-labeled proteins in solution
    • Muhandiram, D. R. et al. Measurement of H-2 T-1 and T-1p relaxation-times in uniformly C-13-Labeled and fractionally H-2-labeled proteins in solution. J. Am. Chem. Soc. 117, 11536-11544 (1995).
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 11536-11544
    • Muhandiram, D.R.1
  • 25
    • 0030473440 scopus 로고    scopus 로고
    • Insights into the local residual entropy of proteins provided by NMR relaxation
    • Li, Z., Raychaudhuri, S. & Wand, A. J. Insights into the local residual entropy of proteins provided by NMR relaxation. Prot. Sci. 5, 2647-2650 (1996).
    • (1996) Prot. Sci , vol.5 , pp. 2647-2650
    • Li, Z.1    Raychaudhuri, S.2    Wand, A.J.3
  • 26
    • 0037137214 scopus 로고    scopus 로고
    • Temperature dependence of the internal dynamics of a calmodulin-peptide complex
    • Lee, A. L. et al. Temperature dependence of the internal dynamics of a calmodulin-peptide complex. Biochemistry 41, 13814-13825 (2002).
    • (2002) Biochemistry , vol.41 , pp. 13814-13825
    • Lee, A.L.1
  • 27
    • 0035942731 scopus 로고    scopus 로고
    • Microscopic origins of entropy, heat capacity and the glass transition in proteins
    • Lee, A. L. & Wand, A. J. Microscopic origins of entropy, heat capacity and the glass transition in proteins. Nature 411, 501-504 (2001).
    • (2001) Nature , vol.411 , pp. 501-504
    • Lee, A.L.1    Wand, A.J.2
  • 28
    • 3042639229 scopus 로고    scopus 로고
    • The origin of protein sidechain order parameter distributions
    • Best, R. B., Clarke, J. & Karplus, M. The origin of protein sidechain order parameter distributions. J. Am. Chem. Soc. 126, 7734-7735 (2004).
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 7734-7735
    • Best, R.B.1    Clarke, J.2    Karplus, M.3
  • 29
    • 0037622537 scopus 로고    scopus 로고
    • CN couplings. J. Am. Chem. Soc. 125, 8959-8966 (2003).
    • CN couplings. J. Am. Chem. Soc. 125, 8959-8966 (2003).
  • 30
    • 18144378006 scopus 로고    scopus 로고
    • What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis
    • Best, R. B., Clarke, J. & Karplus, M. What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis. J. Mol. Biol. 349, 185-203 (2005).
    • (2005) J. Mol. Biol , vol.349 , pp. 185-203
    • Best, R.B.1    Clarke, J.2    Karplus, M.3
  • 31
    • 0037053380 scopus 로고    scopus 로고
    • A direct test of the reductionist approach to structural studies of calmodulin activity: Relevance of peptide models of target proteins
    • Kranz, J. K. et al. A direct test of the reductionist approach to structural studies of calmodulin activity: relevance of peptide models of target proteins. J. Biol. Chem. 277, 16351-16354 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 16351-16354
    • Kranz, J.K.1
  • 32
    • 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, 4546-4559 (1982).
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 33
    • 0024402002 scopus 로고
    • Model-independent and model-dependent analysis of the global and internal dynamics of cyclosporine-A
    • Dellwo, M. J. & Wand, A. J. Model-independent and model-dependent analysis of the global and internal dynamics of cyclosporine-A. J. Am. Chem. Soc. 111, 4571-4578 (1989).
    • (1989) J. Am. Chem. Soc , vol.111 , pp. 4571-4578
    • Dellwo, M.J.1    Wand, A.J.2
  • 34
    • 0018734781 scopus 로고
    • On optimal and data-based histograms
    • Scott, D. On optimal and data-based histograms. Biometrika 10, 605-610 (1979).
    • (1979) Biometrika , vol.10 , pp. 605-610
    • Scott, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.