메뉴 건너뛰기




Volumn 18, Issue 4, 2009, Pages 782-791

Structure of dystrophia myotonica protein kinase

Author keywords

Active sites; BIM; Bisindolylmaleimide; Crystallization; Crystallography; DMPK; Enzyme inhibitors; enzymes; Kinase; Myotonic dystrophy; Protein crystallization; Protein structures; Structure

Indexed keywords

BISINDOLYLMALEIMIDE; BISINDOLYLMALEIMIDE 8; MYOTONIC DYSTROPHY PROTEIN KINASE; RHO KINASE; UNCLASSIFIED DRUG;

EID: 63449137654     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.82     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 2342461060 scopus 로고    scopus 로고
    • Myotonic dystrophy: RNA Pathogenesis Comes into Focus
    • Ranum LPW, Day JW (2004) Myotonic dystrophy: RNA Pathogenesis Comes into Focus. Am J Hum Genet 74: 793-804.
    • (2004) Am J Hum Genet , vol.74 , pp. 793-804
    • Ranum, L.P.W.1    Day, J.W.2
  • 2
    • 15044354661 scopus 로고    scopus 로고
    • RNA pathogenesis of the myotonic dystrophies
    • Day JW, Ranum LPW (2005) RNA pathogenesis of the myotonic dystrophies. Neuromuscular Disord 15:5-16.
    • (2005) Neuromuscular Disord , vol.15 , pp. 5-16
    • Day, J.W.1    Ranum, L.P.W.2
  • 3
    • 0344531040 scopus 로고    scopus 로고
    • Transgenic mouse models for myotonic dystrophy type 1 (DMi)
    • Wans ink DG, Wieringa B (2003) Transgenic mouse models for myotonic dystrophy type 1 (DMi), Cytogenet Genome Res 100:230-242.
    • (2003) Cytogenet Genome Res , vol.100 , pp. 230-242
    • Wans ink, D.G.1    Wieringa, B.2
  • 8
    • 0036537492 scopus 로고    scopus 로고
    • Three proteins, MBNL, MBLL and MBXL, co-localize in vivo with nuclear foci of expanded-repeat transcripts in DMi and DM2 cells
    • Fardaei M, Rogers MT, Thorpe HM, Larkin K, Hamshere MG, Harper PS, Brook JD (2002) Three proteins, MBNL, MBLL and MBXL, co-localize in vivo with nuclear foci of expanded-repeat transcripts in DMi and DM2 cells. Hum Mol Genet 11:805-814.
    • (2002) Hum Mol Genet , vol.11 , pp. 805-814
    • Fardaei, M.1    Rogers, M.T.2    Thorpe, H.M.3    Larkin, K.4    Hamshere, M.G.5    Harper, P.S.6    Brook, J.D.7
  • 9
    • 40649083064 scopus 로고    scopus 로고
    • Expanded CTG repeats within the DMPK 3' UTR causes severe skeletal muscle wasting in an inducible mouse model for myotonic dystrophy
    • Orengo JP, Chambon P, Metzger D, Mosier DR, Snipes GJ, Cooper TA (2008) Expanded CTG repeats within the DMPK 3' UTR causes severe skeletal muscle wasting in an inducible mouse model for myotonic dystrophy. PNAS 105:2646-2651.
    • (2008) PNAS , vol.105 , pp. 2646-2651
    • Orengo, J.P.1    Chambon, P.2    Metzger, D.3    Mosier, D.R.4    Snipes, G.J.5    Cooper, T.A.6
  • 14
    • 42649084007 scopus 로고    scopus 로고
    • Llagostera E, Catalucci D, Marti L, Liesa M, Camps M, Ciaraldi TP, ondo R, Reddy S, Dillmann WH, Palacin M, Zorzano A, Ruiz-Lozano P, Gomis R, Kaliman P (2007) Role of myotonic dystrophy protein kinase (DMPK) in glucose homeostasis and muscle insulin action. PLo S ONE 2:e1134.
    • Llagostera E, Catalucci D, Marti L, Liesa M, Camps M, Ciaraldi TP, ondo R, Reddy S, Dillmann WH, Palacin M, Zorzano A, Ruiz-Lozano P, Gomis R, Kaliman P (2007) Role of myotonic dystrophy protein kinase (DMPK) in glucose homeostasis and muscle insulin action. PLo S ONE 2:e1134.
  • 16
    • 0035970790 scopus 로고    scopus 로고
    • Myotonic dystrophy protein kinase phosphoryiates the myosin phosphatase targetting subu- nit and inhibits myosin phosphatase activity
    • Murányi A, Zhang R, Liu F, Hirano K, Ito M, Epstein HF, Hartshorne DJ (2001) Myotonic dystrophy protein kinase phosphoryiates the myosin phosphatase targetting subu- nit and inhibits myosin phosphatase activity. FEBS Lett 493:80-84.
    • (2001) FEBS Lett , vol.493 , pp. 80-84
    • Murányi, A.1    Zhang, R.2    Liu, F.3    Hirano, K.4    Ito, M.5    Epstein, H.F.6    Hartshorne, D.J.7
  • 18
    • 0034162839 scopus 로고    scopus 로고
    • Constitutive and regulated modes of splicing produce six major myotonic dystrophy protein kinase (DMPK) isoforms with distinct properties
    • Groenen, P.J.T.A., Wansink DG, Coerwinkel MM, van den Broek W, Jansen G, Wieringa B (2000) Constitutive and regulated modes of splicing produce six major myotonic dystrophy protein kinase (DMPK) isoforms with distinct properties. Hum Mol Genet 9:605-616.
    • (2000) Hum Mol Genet , vol.9 , pp. 605-616
    • Groenen, P.J.T.A.1    Wansink, D.G.2    Coerwinkel, M.M.3    van den Broek, W.4    Jansen, G.5    Wieringa, B.6
  • 20
    • 0035079891 scopus 로고    scopus 로고
    • Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related cdc42-binding kinase α
    • Tan I, Seow KT, Lim L, Leung T (2001) Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related cdc42-binding kinase α. Mol Cell Biol 21:2767-2778.
    • (2001) Mol Cell Biol , vol.21 , pp. 2767-2778
    • Tan, I.1    Seow, K.T.2    Lim, L.3    Leung, T.4
  • 21
    • 10644234702 scopus 로고    scopus 로고
    • New insights into the structure-function relationships of Rho- associated kinase: A thermodynamic and hydrodynamic study of the dimer-to-monomer transition and its kinetic implications
    • Doran JD, Liu X, Taslimi P, Saadat A, Fox T (2004) New insights into the structure-function relationships of Rho- associated kinase: a thermodynamic and hydrodynamic study of the dimer-to-monomer transition and its kinetic implications. Biochem J 384:255-262.
    • (2004) Biochem J , vol.384 , pp. 255-262
    • Doran, J.D.1    Liu, X.2    Taslimi, P.3    Saadat, A.4    Fox, T.5
  • 23
    • 33644837834 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of rho-kinase by dimerization and its inhibition by fasudil
    • Yamaguchi H, Kasa M, Amano M, Kaibuchi K, Hakoshima T (2006) Molecular mechanism for the regulation of rho-kinase by dimerization and its inhibition by fasudil. Structure 14:589-600.
    • (2006) Structure , vol.14 , pp. 589-600
    • Yamaguchi, H.1    Kasa, M.2    Amano, M.3    Kaibuchi, K.4    Hakoshima, T.5
  • 25
    • 33846590132 scopus 로고    scopus 로고
    • The hallmark of AGC kinase functional divergence is its C-terminal tail, a cis-acting regulatory module
    • Kannan N, Haste N, Taylor SS, Neuwald AF (2007) The hallmark of AGC kinase functional divergence is its C-terminal tail, a cis-acting regulatory module. PNAS 104: 1272-1277.
    • (2007) PNAS , vol.104 , pp. 1272-1277
    • Kannan, N.1    Haste, N.2    Taylor, S.S.3    Neuwald, A.F.4
  • 26
    • 0031571091 scopus 로고    scopus 로고
    • A binary complex of the catalytix subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility
    • Narayana N, Cox S, Xuong, N-H, Ten Eyck LF, Taylor SS (1997) A binary complex of the catalytix subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility. Structure 5:921-935.
    • (1997) Structure , vol.5 , pp. 921-935
    • Narayana, N.1    Cox, S.2    Xuong, N.-H.3    Ten Eyck, L.F.4    Taylor, S.S.5
  • 28
    • 36448934106 scopus 로고    scopus 로고
    • Zhao B, Lehr R. Smallwood AM. Ho TF', Maley K, Randall T, Head MS, Koretke KK, Schnackenberg CG (2007) Crystal structure of the kinase domain of serum and glucocorticoid-regulated kinase 1 in complex with AMP-PNP. Prot Sci 16:1-9.
    • Zhao B, Lehr R. Smallwood AM. Ho TF', Maley K, Randall T, Head MS, Koretke KK, Schnackenberg CG (2007) Crystal structure of the kinase domain of serum and glucocorticoid-regulated kinase 1 in complex with AMP-PNP. Prot Sci 16:1-9.
  • 29
    • 24644488646 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif
    • Messerschmidt A, Macieira S, Velarde M, Bädeker M, Benda C, Jestel A, Brandsterter H, Neuefeind T, Blaesse M (2005) Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif. J Mol Biol 352:918-931.
    • (2005) J Mol Biol , vol.352 , pp. 918-931
    • Messerschmidt, A.1    Macieira, S.2    Velarde, M.3    Bädeker, M.4    Benda, C.5    Jestel, A.6    Brandsterter, H.7    Neuefeind, T.8    Blaesse, M.9
  • 30
    • 0034705685 scopus 로고    scopus 로고
    • Rac-1 and Raf-1 kinases, components of distinct signaling pathways, activate myotonic dystrophy protein kinase
    • Shimizu M, Wang W, Walch ET, Dunne PW, Epstein HF (2000) Rac-1 and Raf-1 kinases, components of distinct signaling pathways, activate myotonic dystrophy protein kinase. FEBS Lett 475:273-277.
    • (2000) FEBS Lett , vol.475 , pp. 273-277
    • Shimizu, M.1    Wang, W.2    Walch, E.T.3    Dunne, P.W.4    Epstein, H.F.5
  • 31
    • 1342304087 scopus 로고    scopus 로고
    • Structural insights into the interaction of ROCK1 with the switch regions of RhoA
    • Dvorsky R, Blumenstein L, Vetter IR, Ahmadian MR (2004) Structural insights into the interaction of ROCK1 with the switch regions of RhoA. J Biol Chem 279:7098- 7104.
    • (2004) J Biol Chem , vol.279 , pp. 7098-7104
    • Dvorsky, R.1    Blumenstein, L.2    Vetter, I.R.3    Ahmadian, M.R.4
  • 32
    • 0034713879 scopus 로고    scopus 로고
    • Myotonic dystrophy protein kinase domains mediate localization, oligomerization, novel catalytic activity, and autoinhibition
    • Bush EW, Helmke SM, Birnbaum RA, Perryman MB (2000) Myotonic dystrophy protein kinase domains mediate localization, oligomerization, novel catalytic activity, and autoinhibition. Biochemistry 39:8480-8490.
    • (2000) Biochemistry , vol.39 , pp. 8480-8490
    • Bush, E.W.1    Helmke, S.M.2    Birnbaum, R.A.3    Perryman, M.B.4
  • 33
    • 57149120091 scopus 로고    scopus 로고
    • Mechanism of multi-site phosphorylation from a ROCK1:RhoE complex structure
    • Komander D, Garg R, Wan PTC, Ridley AJ, Barford D (2008) Mechanism of multi-site phosphorylation from a ROCK1:RhoE complex structure. EMBO J 27:3175-3185.
    • (2008) EMBO J , vol.27 , pp. 3175-3185
    • Komander, D.1    Garg, R.2    Wan, P.T.C.3    Ridley, A.J.4    Barford, D.5
  • 36
    • 0033212815 scopus 로고    scopus 로고
    • Leslie AGW (1999) Integration of macromolecular diffraction data. Acta Crystallogr. 055:1696-1702.
    • Leslie AGW (1999) Integration of macromolecular diffraction data. Acta Crystallogr. 055:1696-1702.
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D50:760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 38
    • 3042613550 scopus 로고    scopus 로고
    • Likelihood- enhanced fast rotation functions
    • Storoni LC, McCoy AJ, Read RJ (2004) Likelihood- enhanced fast rotation functions. Acta Crystallogr D60: 432-438.
    • (2004) Acta Crystallogr , vol.D60 , pp. 432-438
    • Storoni, L.C.1    McCoy, A.J.2    Read, R.J.3
  • 39
    • 13244281317 scopus 로고    scopus 로고
    • COOT: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) COOT: model-building tools for molecular graphics. Acta Crystallogr D6o:2126-2132.
    • (2004) Acta Crystallogr , vol.D6o , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 41
    • 33744809773 scopus 로고    scopus 로고
    • Macromolecular size-and- shape distributions by sedimentation velocity analytical ultracentrifugation
    • Brown PH, Schuck P (2006) Macromolecular size-and- shape distributions by sedimentation velocity analytical ultracentrifugation. Biophys J 90:4651-4661.
    • (2006) Biophys J , vol.90 , pp. 4651-4661
    • Brown, P.H.1    Schuck, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.