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Volumn 42, Issue 1, 2014, Pages 139-144

Allosteric linkers in cAMP signalling

Author keywords

Allostery; CAMP; CGMP; Covariance; NMR; Protein dynamics; Singular value decomposition (SVD)

Indexed keywords

CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; PHOSPHOTRANSFERASE INHIBITOR;

EID: 84893289817     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20130257     Document Type: Article
Times cited : (16)

References (24)
  • 1
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • Kuriyan, J. and Eisenberg, D. (2007) The origin of protein interactions and allostery in colocalization. Nature 450, 983-990
    • (2007) Nature , vol.450 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 3
    • 79959429733 scopus 로고    scopus 로고
    • Protein regulation: The statistical theory of allostery
    • Vendruscolo, M. (2011) Protein regulation: the statistical theory of allostery. Nat. Chem. Biol. 7, 411-412
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 411-412
    • Vendruscolo, M.1
  • 5
    • 84869746585 scopus 로고    scopus 로고
    • The auto-inhibitory role of the EPAC hinge helix as mapped by NMR
    • Selvaratnam, R., Mazhab-Jafari, M.T., Das, R. and Melacini, G. (2012) The auto-inhibitory role of the EPAC hinge helix as mapped by NMR. PLoS ONE 7, e487076
    • (2012) PLoS ONE , vol.7
    • Selvaratnam, R.1    Mazhab-Jafari, M.T.2    Das, R.3    Melacini, G.4
  • 6
    • 77952068200 scopus 로고    scopus 로고
    • Communication between tandem cAMP binding domains in the regulatory subunit of protein kinase A-Ia as revealed by domain-silencing mutations
    • McNicholl, E.T., Das, R., SilDas, S., Taylor, S.S. and Melacini, G. (2010) Communication between tandem cAMP binding domains in the regulatory subunit of protein kinase A-Ia as revealed by domain-silencing mutations. J. Biol. Chem. 285, 15523-15537
    • (2010) J. Biol. Chem. , vol.285 , pp. 15523-15537
    • McNicholl, E.T.1    Das, R.2    Sildas, S.3    Taylor, S.S.4    Melacini, G.5
  • 7
    • 0034269240 scopus 로고    scopus 로고
    • Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation
    • Aghazadeh, B., Lowry, W.E., Huang, X.Y. and Rosen, M.K. (2000) Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation. Cell 102, 625-633
    • (2000) Cell , vol.102 , pp. 625-633
    • Aghazadeh, B.1    Lowry, W.E.2    Huang, X.Y.3    Rosen, M.K.4
  • 8
    • 82755171820 scopus 로고    scopus 로고
    • Role of dynamics in the autoinhibition and activation of the exchange protein directly activated by cyclic AMP (EPAC)
    • VanSchouwen, B., Selavaratnam, R., Fogolari, F. and Melacini, G. (2011) Role of dynamics in the autoinhibition and activation of the exchange protein directly activated by cyclic AMP (EPAC). J. Biol. Chem. 286, 42655-42669
    • (2011) J. Biol. Chem. , vol.286 , pp. 42655-42669
    • Vanschouwen, B.1    Selavaratnam, R.2    Fogolari, F.3    Melacini, G.4
  • 9
    • 64849111005 scopus 로고    scopus 로고
    • Sending signals dynamically
    • Smock, R.G. and Gierasch, L.M. (2009) Sending signals dynamically. Science 324, 198-203
    • (2009) Science , vol.324 , pp. 198-203
    • Smock, R.G.1    Gierasch, L.M.2
  • 10
    • 84856748688 scopus 로고    scopus 로고
    • The projection analysis of NMR chemical shifts reveals extended EPAC autoinhibition determinants
    • Selvaratnam, R., VanSchouwen, B., Fogolari, F., Mazhab-Jafari, M.T., Das, R. and Melacini, G. (2012) The projection analysis of NMR chemical shifts reveals extended EPAC autoinhibition determinants. Biophys. J. 102, 630-639
    • (2012) Biophys. J. , vol.102 , pp. 630-639
    • Selvaratnam, R.1    Vanschouwen, B.2    Fogolari, F.3    Mazhab-Jafari, M.T.4    Das, R.5    Melacini, G.6
  • 11
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr, D.D., Nussinov, R. and Wright, P.E. (2009) The role of dynamic conformational ensembles in biomolecular recognition. Nat. Chem. Biol. 5, 789-796
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 12
    • 78650486391 scopus 로고    scopus 로고
    • Structural basis for regulation of the Crk signaling protein by a proline switch
    • Sarkar, P., Saleh, T., Tzeng, S.R., Birge, R.B. and Kalodimos, C.G. (2011) Structural basis for regulation of the Crk signaling protein by a proline switch. Nat. Chem. Biol. 7, 51-57
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 51-57
    • Sarkar, P.1    Saleh, T.2    Tzeng, S.R.3    Birge, R.B.4    Kalodimos, C.G.5
  • 14
    • 79960189344 scopus 로고    scopus 로고
    • Dynamic allostery: Linkers are not merely flexible
    • Ma, B., Tsai, C.J., Haliloglu, T. and Nussinov, R. (2011) Dynamic allostery: linkers are not merely flexible. Structure 19, 907-917
    • (2011) Structure , vol.19 , pp. 907-917
    • Ma, B.1    Tsai, C.J.2    Haliloglu, T.3    Nussinov, R.4
  • 15
    • 79955565642 scopus 로고    scopus 로고
    • Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones
    • Zhuravleva, A. and Gierasch, L.M. (2011) Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proc. Natl. Acad. Sci. U.S.A. 108, 6987-6992
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 6987-6992
    • Zhuravleva, A.1    Gierasch, L.M.2
  • 16
    • 13244291292 scopus 로고    scopus 로고
    • Crystal structure of a complex between the catalytic and regulatory (RIα) subunits of PKA
    • Kim, C., Xuong, N.H. and Taylor, S.S. (2005) Crystal structure of a complex between the catalytic and regulatory (RIα) subunits of PKA. Science 307, 690-696
    • (2005) Science , vol.307 , pp. 690-696
    • Kim, C.1    Xuong, N.H.2    Taylor, S.S.3
  • 17
    • 2542523982 scopus 로고    scopus 로고
    • Crystal structures of RIα subunit of cyclic adenosine 5′-monophosphate (cAMP)-dependent protein kinase complexed with (Rp)-adenosine 3′,5′-cyclic monophosphothioate and (Sp)-adenosine 3′,5′-cyclic monophosphothioate, the phosphothioate analogues of cAMP
    • Wu, J., Jones, J.M., Nguyen-Huu, X., Ten Eyck, L.F. and Taylor, S.S. (2004) Crystal structures of RIα subunit of cyclic adenosine 5′-monophosphate (cAMP)-dependent protein kinase complexed with (Rp)-adenosine 3′,5′-cyclic monophosphothioate and (Sp)-adenosine 3′,5′-cyclic monophosphothioate, the phosphothioate analogues of cAMP. Biochemistry 43, 6620-6629
    • (2004) Biochemistry , vol.43 , pp. 6620-6629
    • Wu, J.1    Jones, J.M.2    Nguyen-Huu, X.3    Ten Eyck, L.F.4    Taylor, S.S.5
  • 18
    • 50349092827 scopus 로고    scopus 로고
    • Entropy-driven cAMP-dependent allosteric control of inhibitory interactions in exchange proteins directly activated by cAMP
    • Das, R., Mazhab-Jafari, M.T., Chowdhury, S., SilDas, S., Selvaratnam, R. and Melacini, G. (2008) Entropy-driven cAMP-dependent allosteric control of inhibitory interactions in exchange proteins directly activated by cAMP. J. Biol. Chem. 283, 19691-19703
    • (2008) J. Biol. Chem. , vol.283 , pp. 19691-19703
    • Das, R.1    Mazhab-Jafari, M.T.2    Chowdhury, S.3    Sildas, S.4    Selvaratnam, R.5    Melacini, G.6
  • 20
    • 77957988475 scopus 로고    scopus 로고
    • Cyclic AMP- and (Rp)-cAMPS-induced conformational changes in a complex of the catalytic and regulatory (RIα) subunits of cyclic AMP-dependent protein kinase
    • Anand, G.S., Krishnamurthy, S., Bishnoi, T., Kornev, A., Taylor, S.S. and Johnson, D.A. (2010) Cyclic AMP- and (Rp)-cAMPS-induced conformational changes in a complex of the catalytic and regulatory (RIα) subunits of cyclic AMP-dependent protein kinase. Mol. Cell. Proteomics 9, 2225-2237
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2225-2237
    • Anand, G.S.1    Krishnamurthy, S.2    Bishnoi, T.3    Kornev, A.4    Taylor, S.S.5    Johnson, D.A.6
  • 23
    • 33846561471 scopus 로고    scopus 로고
    • Practical aspects of 1H transverse paramagnetic relaxation enhancement measurements on macromolecules
    • Iwahara, J., Tang, C. and Clore, G.M. (2007) Practical aspects of 1H transverse paramagnetic relaxation enhancement measurements on macromolecules. J. Magn. Reson. 184, 185-195
    • (2007) J. Magn. Reson. , vol.184 , pp. 185-195
    • Iwahara, J.1    Tang, C.2    Clore, G.M.3
  • 24
    • 34548611290 scopus 로고    scopus 로고
    • PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation
    • Kim, C., Cheng, C.Y., Saldanha, S.A. and Taylor, S.S. (2007) PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation. Cell 130, 1032-1043
    • (2007) Cell , vol.130 , pp. 1032-1043
    • Kim, C.1    Cheng, C.Y.2    Saldanha, S.A.3    Taylor, S.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.