메뉴 건너뛰기




Volumn 17, Issue 1, 2005, Pages 69-82

Crystal structure and interactions of the PAS repeat region of the Drosophila clock protein PERIOD

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; INSECT PROTEIN; PROTEIN PERIOD; UNCLASSIFIED DRUG;

EID: 19944426818     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.11.022     Document Type: Article
Times cited : (84)

References (53)
  • 1
    • 0029144661 scopus 로고
    • Evaluation of protein 3-D structure prediction: Comparison of modelled and X-ray structure of an alkaline serine protease
    • Aehle W., Sobek H., Schomburg D. Evaluation of protein 3-D structure prediction. comparison of modelled and X-ray structure of an alkaline serine protease J. Biotechnol. 41:1995;211-219
    • (1995) J. Biotechnol. , vol.41 , pp. 211-219
    • Aehle, W.1    Sobek, H.2    Schomburg, D.3
  • 2
    • 0036178045 scopus 로고    scopus 로고
    • Control of intracellular dynamics of mammalian period proteins by casein kinase I epsilon (CKIepsilon) and CKIdelta in cultured cells
    • Akashi M., Tsuchiya Y., Yoshino T., Nishida E. Control of intracellular dynamics of mammalian period proteins by casein kinase I epsilon (CKIepsilon) and CKIdelta in cultured cells. Mol. Cell. Biol. 22:2002;1693-1703
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1693-1703
    • Akashi, M.1    Tsuchiya, Y.2    Yoshino, T.3    Nishida, E.4
  • 4
    • 0036774056 scopus 로고    scopus 로고
    • Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation
    • Amezcua C.A., Harper S.M., Rutter J., Gardner K.H. Structure and interactions of PAS kinase N-terminal PAS domain. model for intramolecular kinase regulation Structure. 10:2002;1349-1361
    • (2002) Structure , vol.10 , pp. 1349-1361
    • Amezcua, C.A.1    Harper, S.M.2    Rutter, J.3    Gardner, K.H.4
  • 5
    • 0026804699 scopus 로고
    • New short period mutations of the Drosophila clock gene per
    • Baylies M.K., Vosshall L.B., Sehgal A., Young M.W. New short period mutations of the Drosophila clock gene per. Neuron. 9:1992;575-581
    • (1992) Neuron , vol.9 , pp. 575-581
    • Baylies, M.K.1    Vosshall, L.B.2    Sehgal, A.3    Young, M.W.4
  • 6
    • 0029110488 scopus 로고
    • 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
    • Borgstahl G.E., Williams D.R., Getzoff E.D. 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor. unusual fold, active site, and chromophore Biochemistry (Mosc.). 34:1995;6278-6287
    • (1995) Biochemistry (Mosc.) , vol.34 , pp. 6278-6287
    • Borgstahl, G.E.1    Williams, D.R.2    Getzoff, E.D.3
  • 9
    • 0038032878 scopus 로고    scopus 로고
    • A novel C-terminal domain of Drosophila PERIOD inhibits dCLOCK: CYCLE-mediated transcription
    • Chang D.C., Reppert S.M. A novel C-terminal domain of Drosophila PERIOD inhibits dCLOCK. CYCLE-mediated transcription Curr. Biol. 13:2003;758-762
    • (2003) Curr. Biol. , vol.13 , pp. 758-762
    • Chang, D.C.1    Reppert, S.M.2
  • 10
    • 0024254817 scopus 로고
    • Interspecific comparison of the period gene of Drosophila reveals large blocks of non-conserved coding DNA
    • Colot H.V., Hall J.C., Rosbash M. Interspecific comparison of the period gene of Drosophila reveals large blocks of non-conserved coding DNA. EMBO J. 7:1988;3929-3937
    • (1988) EMBO J. , vol.7 , pp. 3929-3937
    • Colot, H.V.1    Hall, J.C.2    Rosbash, M.3
  • 11
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction
    • Crosson S., Moffat K. Structure of a flavin-binding plant photoreceptor domain. insights into light-mediated signal transduction Proc. Natl. Acad. Sci. USA. 98:2001;2995-3000
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2995-3000
    • Crosson, S.1    Moffat, K.2
  • 12
    • 0028838141 scopus 로고
    • Temporally regulated nuclear entry of the Drosophila period protein contributes to the circadian clock
    • Curtin K.D., Huang Z.J., Rosbash M. Temporally regulated nuclear entry of the Drosophila period protein contributes to the circadian clock. Neuron. 14:1995;365-372
    • (1995) Neuron , vol.14 , pp. 365-372
    • Curtin, K.D.1    Huang, Z.J.2    Rosbash, M.3
  • 13
    • 0033593306 scopus 로고    scopus 로고
    • Molecular bases for circadian clocks
    • Dunlap J.C. Molecular bases for circadian clocks. Cell. 96:1999;271-290
    • (1999) Cell , vol.96 , pp. 271-290
    • Dunlap, J.C.1
  • 14
    • 0346734132 scopus 로고    scopus 로고
    • Structural basis for PAS domain heterodimerization in the basic helix-loop-helix-PAS transcription factor hypoxia-inducible factor
    • Erbel P.J., Card P.B., Karakuzu O., Bruick R.K., Gardner K.H. Structural basis for PAS domain heterodimerization in the basic helix-loop-helix-PAS transcription factor hypoxia-inducible factor. Proc. Natl. Acad. Sci. USA. 100:2003;15504-15509
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15504-15509
    • Erbel, P.J.1    Card, P.B.2    Karakuzu, O.3    Bruick, R.K.4    Gardner, K.H.5
  • 15
    • 0037380836 scopus 로고    scopus 로고
    • Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii
    • Fedorov R., Schlichting I., Hartmann E., Domratcheva T., Fuhrmann M., Hegemann P. Crystal structures and molecular mechanism of a light-induced signaling switch. the Phot-LOV1 domain from Chlamydomonas reinhardtii Biophys. J. 84:2003;2474-2482
    • (2003) Biophys. J. , vol.84 , pp. 2474-2482
    • Fedorov, R.1    Schlichting, I.2    Hartmann, E.3    Domratcheva, T.4    Fuhrmann, M.5    Hegemann, P.6
  • 16
    • 0038243196 scopus 로고    scopus 로고
    • POVScript+ a program for model and data visualization using persistence of vision ray-tracing
    • Fenn T.D., Ringe D., Petsko G.A. POVScript+. a program for model and data visualization using persistence of vision ray-tracing J. Appl. Crystallogr. 36:2003;944-947
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 944-947
    • Fenn, T.D.1    Ringe, D.2    Petsko, G.A.3
  • 17
  • 18
    • 0028882226 scopus 로고
    • Isolation of timeless by PER protein interaction: Defective interaction between timeless protein and long-period mutant PERL
    • Gekakis N., Saez L., Delahaye-Brown A.M., Myers M.P., Sehgal A., Young M.W., Weitz C.J. Isolation of timeless by PER protein interaction. defective interaction between timeless protein and long-period mutant PERL Science. 270:1995;811-815
    • (1995) Science , vol.270 , pp. 811-815
    • Gekakis, N.1    Saez, L.2    Delahaye-Brown, A.M.3    Myers, M.P.4    Sehgal, A.5    Young, M.W.6    Weitz, C.J.7
  • 19
    • 0036713612 scopus 로고    scopus 로고
    • Central and peripheral circadian oscillator mechanisms in flies and mammals
    • Glossop N.R., Hardin P.E. Central and peripheral circadian oscillator mechanisms in flies and mammals. J. Cell Sci. 115:2002;3369-3377
    • (2002) J. Cell Sci. , vol.115 , pp. 3369-3377
    • Glossop, N.R.1    Hardin, P.E.2
  • 21
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper S.M., Neil L.C., Gardner K.H. Structural basis of a phototropin light switch. Science. 301:2003;1541-1544
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 22
    • 0030887045 scopus 로고    scopus 로고
    • Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway
    • Hogenesch J.B., Chan W.K., Jackiw V.H., Brown R.C., Gu Y.Z., Pray-Grant M., Perdew G.H., Bradfield C.A. Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway. J. Biol. Chem. 272:1997;8581-8593
    • (1997) J. Biol. Chem. , vol.272 , pp. 8581-8593
    • Hogenesch, J.B.1    Chan, W.K.2    Jackiw, V.H.3    Brown, R.C.4    Gu, Y.Z.5    Pray-Grant, M.6    Perdew, G.H.7    Bradfield, C.A.8
  • 23
    • 0027184569 scopus 로고
    • PAS is a dimerization domain common to Drosophila period and several transcription factors
    • Huang Z.J., Edery I., Rosbash M. PAS is a dimerization domain common to Drosophila period and several transcription factors. Nature. 364:1993;259-262
    • (1993) Nature , vol.364 , pp. 259-262
    • Huang, Z.J.1    Edery, I.2    Rosbash, M.3
  • 24
    • 0028933507 scopus 로고
    • PER protein interactions and temperature compensation of a circadian clock in Drosophila
    • Huang Z.J., Curtin K.D., Rosbash M. PER protein interactions and temperature compensation of a circadian clock in Drosophila. Science. 267:1995;1169-1172
    • (1995) Science , vol.267 , pp. 1169-1172
    • Huang, Z.J.1    Curtin, K.D.2    Rosbash, M.3
  • 25
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26:1993;795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 26
    • 4444260675 scopus 로고    scopus 로고
    • Interaction of the PAS B domain with HSP90 accelerates hypoxia-inducible factor-1alpha stabilization
    • Katschinski D., Le L., Schindler S., Thomas T., Voss A., Wenger R. Interaction of the PAS B domain with HSP90 accelerates hypoxia-inducible factor-1alpha stabilization. Cell. Physiol. Biochem. 14:2004;351-360
    • (2004) Cell. Physiol. Biochem. , vol.14 , pp. 351-360
    • Katschinski, D.1    Le, L.2    Schindler, S.3    Thomas, T.4    Voss, A.5    Wenger, R.6
  • 28
    • 0034042294 scopus 로고    scopus 로고
    • Molecular genetics of circadian rhythms in mammals
    • King D.P., Takahashi J.S. Molecular genetics of circadian rhythms in mammals. Annu. Rev. Neurosci. 23:2000;713-742
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 713-742
    • King, D.P.1    Takahashi, J.S.2
  • 29
    • 0032504041 scopus 로고    scopus 로고
    • The Drosophila clock gene double-time encodes a protein closely related to human casein kinase Iepsilon
    • Kloss B., Price J.L., Saez L., Blau J., Rothenfluh A., Wesley C.S., Young M.W. The Drosophila clock gene double-time encodes a protein closely related to human casein kinase Iepsilon. Cell. 94:1998;97-107
    • (1998) Cell , vol.94 , pp. 97-107
    • Kloss, B.1    Price, J.L.2    Saez, L.3    Blau, J.4    Rothenfluh, A.5    Wesley, C.S.6    Young, M.W.7
  • 31
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24:1991;946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 32
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • S.E. Harding, A.J. Rowe, & J.C. Horton. Cambridge, UK: The Royal Society of Chemistry
    • Laue T.M., Shah B.D., Ridgeway T.M., Pelletier S. Computer-aided interpretation of analytical sedimentation data for proteins. Harding S.E., Rowe A.J., Horton J.C. Analytical Ultracentrifugation in Biochemistry and Polymer Science. 1992;90-125 The Royal Society of Chemistry, Cambridge, UK
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.4
  • 33
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence M.C., Colman P.M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234:1993;946-950
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 35
    • 0035141217 scopus 로고    scopus 로고
    • Wild-type circadian rhythmicity is dependent on closely spaced e boxes in the Drosophila timeless promoter
    • McDonald M.J., Rosbash M., Emery P. Wild-type circadian rhythmicity is dependent on closely spaced E boxes in the Drosophila timeless promoter. Mol. Cell. Biol. 21:2001;1207-1217
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1207-1217
    • McDonald, M.J.1    Rosbash, M.2    Emery, P.3
  • 36
    • 0032790081 scopus 로고    scopus 로고
    • XtalView Xfit: A versatile program for manipulating atomic coordinates and electron density
    • Mcree D.E. XtalView Xfit. a versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125:1999;156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 37
    • 0028057108 scopus 로고
    • Raster3D Version 2.0: A program for photorealistic molecular graphics
    • Merritt E.A., Murphy M.E.P. Raster3D Version 2.0. a program for photorealistic molecular graphics Acta Crystallogr. D Biol. Crystallogr. 50:1994;869-873
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 38
    • 0030740207 scopus 로고    scopus 로고
    • The murine Sim-2 gene product inhibits transcription by active repression and functional interference
    • Moffett P., Reece M., Pelletier J. The murine Sim-2 gene product inhibits transcription by active repression and functional interference. Mol. Cell. Biol. 17:1997;4933-4947
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4933-4947
    • Moffett, P.1    Reece, M.2    Pelletier, J.3
  • 39
    • 0032567106 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the HERG potassium channel N terminus: A eukaryotic PAS domain
    • Morais Cabral J.H., Lee A., Cohen S.L., Chait B.T., Li M., MacKinnon R. Crystal structure and functional analysis of the HERG potassium channel N terminus. a eukaryotic PAS domain Cell. 95:1998;649-655
    • (1998) Cell , vol.95 , pp. 649-655
    • Morais Cabral, J.H.1    Lee, A.2    Cohen, S.L.3    Chait, B.T.4    Li, M.5    MacKinnon, R.6
  • 40
    • 0442319504 scopus 로고    scopus 로고
    • The doubletime and CKII kinases collaborate to potentiate Drosophila PER transcriptional repressor activity
    • Nawathean P., Rosbash M. The doubletime and CKII kinases collaborate to potentiate Drosophila PER transcriptional repressor activity. Mol. Cell. 13:2004;213-223
    • (2004) Mol. Cell , vol.13 , pp. 213-223
    • Nawathean, P.1    Rosbash, M.2
  • 41
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 42
    • 0032503969 scopus 로고    scopus 로고
    • Double-time is a novel Drosophila clock gene that regulates PERIOD protein accumulation
    • Price J.L., Blau J., Rothenfluh A., Abodeely M., Kloss B., Young M.W. double-time is a novel Drosophila clock gene that regulates PERIOD protein accumulation. Cell. 94:1998;83-95
    • (1998) Cell , vol.94 , pp. 83-95
    • Price, J.L.1    Blau, J.2    Rothenfluh, A.3    Abodeely, M.4    Kloss, B.5    Young, M.W.6
  • 43
    • 0035954257 scopus 로고    scopus 로고
    • Light-dependent interaction between Drosophila CRY and the clock protein PER mediated by the carboxy terminus of CRY
    • Rosato E., Codd V., Mazzotta G., Piccin A., Zordan M., Costa R., Kyriacou C.P. Light-dependent interaction between Drosophila CRY and the clock protein PER mediated by the carboxy terminus of CRY. Curr. Biol. 11:2001;909-917
    • (2001) Curr. Biol. , vol.11 , pp. 909-917
    • Rosato, E.1    Codd, V.2    Mazzotta, G.3    Piccin, A.4    Zordan, M.5    Costa, R.6    Kyriacou, C.P.7
  • 44
    • 0033711617 scopus 로고    scopus 로고
    • A TIMELESS-independent function for PERIOD proteins in the Drosophila clock
    • Rothenfluh A., Young M.W., Saez L. A TIMELESS-independent function for PERIOD proteins in the Drosophila clock. Neuron. 26:2000;505-514
    • (2000) Neuron , vol.26 , pp. 505-514
    • Rothenfluh, A.1    Young, M.W.2    Saez, L.3
  • 45
    • 0030293638 scopus 로고    scopus 로고
    • Regulation of nuclear entry of the Drosophila clock proteins period and timeless
    • Saez L., Young M.W. Regulation of nuclear entry of the Drosophila clock proteins period and timeless. Neuron. 17:1996;911-920
    • (1996) Neuron , vol.17 , pp. 911-920
    • Saez, L.1    Young, M.W.2
  • 47
    • 0037101628 scopus 로고    scopus 로고
    • Sequential nuclear accumulation of the clock proteins period and timeless in the pacemaker neurons of Drosophila melanogaster
    • Shafer O.T., Rosbash M., Truman J.W. Sequential nuclear accumulation of the clock proteins period and timeless in the pacemaker neurons of Drosophila melanogaster. J. Neurosci. 22:2002;5946-5954
    • (2002) J. Neurosci. , vol.22 , pp. 5946-5954
    • Shafer, O.T.1    Rosbash, M.2    Truman, J.W.3
  • 48
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor B.L., Zhulin I.B. PAS domains. internal sensors of oxygen, redox potential, and light Microbiol. Mol. Biol. Rev. 63:1999;479-506
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 49
    • 0027968068 scopus 로고
    • Clustal w: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. Clustal w. improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22:1994;4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 52
    • 0029979174 scopus 로고    scopus 로고
    • A light-entrainment mechanism for the Drosophila circadian clock
    • Zeng H., Qian Z., Myers M.P., Rosbash M. A light-entrainment mechanism for the Drosophila circadian clock. Nature. 380:1996;129-135
    • (1996) Nature , vol.380 , pp. 129-135
    • Zeng, H.1    Qian, Z.2    Myers, M.P.3    Rosbash, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.