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Volumn 294, Issue 4, 1999, Pages 1041-1049

Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53

Author keywords

FHA domain; Phosphopeptide; Phosphoprotein; Rad53; Rad9

Indexed keywords

AMINO ACID; PHOSPHOPEPTIDE;

EID: 0033544711     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3313     Document Type: Article
Times cited : (98)

References (35)
  • 1
    • 0027968012 scopus 로고
    • The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast
    • Allen J., Zhou Z., Siede W., Friedberg E., Elledge S. The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast. Genes Dev. 8:1994;2401-2415.
    • (1994) Genes Dev. , vol.8 , pp. 2401-2415
    • Allen, J.1    Zhou, Z.2    Siede, W.3    Friedberg, E.4    Elledge, S.5
  • 2
    • 0033616828 scopus 로고    scopus 로고
    • A human Cds1-related kinase that functions downstream of ATM protein in the cellular response to DNA damage
    • Brown A., Lee C., Schwarz J., Mitiku N. H. P.-W., Chung J. A human Cds1-related kinase that functions downstream of ATM protein in the cellular response to DNA damage. Proc. Natl Acad. Sci. USA. 96:1999;3745-3750.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3745-3750
    • Brown, A.1    Lee, C.2    Schwarz, J.3    Mitiku, N.H.P.-W.4    Chung, J.5
  • 3
    • 0000939457 scopus 로고
    • The three-dimensional structure of α1-purothionin in solution: Combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics
    • Clore G. M., Nilges M., Sukumaran D. K., Brünger A. T., Karplus M., Gronenborn A. M. The three-dimensional structure of α1-purothionin in solution: combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J. 5:1986;2729-2735.
    • (1986) EMBO J. , vol.5 , pp. 2729-2735
    • Clore, G.M.1    Nilges, M.2    Sukumaran, D.K.3    Brünger, A.T.4    Karplus, M.5    Gronenborn, A.M.6
  • 4
    • 0023475020 scopus 로고
    • Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics
    • Clore G., Gronenborn A., Nilges M., Ryan C. Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry. 26:1987;8012-8023.
    • (1987) Biochemistry , vol.26 , pp. 8012-8023
    • Clore, G.1    Gronenborn, A.2    Nilges, M.3    Ryan, C.4
  • 5
    • 0033197541 scopus 로고    scopus 로고
    • The FHA domain is a modular phosphopeptide recognition motif
    • Durocher D., Henckel J., Fersht A. R., Jackson S. P. The FHA domain is a modular phosphopeptide recognition motif. Mol. Cell. 4:1999;387-394.
    • (1999) Mol. Cell , vol.4 , pp. 387-394
    • Durocher, D.1    Henckel, J.2    Fersht, A.R.3    Jackson, S.P.4
  • 6
    • 0027502504 scopus 로고
    • Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck
    • Eck M., Shoelson S., Harrison S. Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck. Nature. 362:1993;87-91.
    • (1993) Nature , vol.362 , pp. 87-91
    • Eck, M.1    Shoelson, S.2    Harrison, S.3
  • 7
    • 0000470905 scopus 로고
    • Heteronuclear three-dimensional NMR spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra
    • Fesik A. W., Zuiderweg E. R. P. Heteronuclear three-dimensional NMR spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra. J. Magn. Reson. 78:1988;588-593.
    • (1988) J. Magn. Reson. , vol.78 , pp. 588-593
    • Fesik, A.W.1    Zuiderweg, E.R.P.2
  • 8
    • 0029360452 scopus 로고
    • The FHA domain: A putative nuclear signalling domain found in protein kinases and transcription factors
    • Hofmann K., Bucher P. The FHA domain: a putative nuclear signalling domain found in protein kinases and transcription factors. Trends Biochem. Sci. 20:1995;347-349.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 347-349
    • Hofmann, K.1    Bucher, P.2
  • 9
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55, 29-32.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 10
    • 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. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 11
    • 0030950608 scopus 로고    scopus 로고
    • Modular peptide recognition domains in eukaryotic signaling
    • Kuriyan J., Cowburn D. Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 26:1997;259-288.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 259-288
    • Kuriyan, J.1    Cowburn, D.2
  • 12
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 13
    • 0026567640 scopus 로고
    • The MRE4 gene encodes a novel protein kinase homologue required for meiotic recombination in Saccharomyces cerevisiae
    • Leem S., Ogawa H. The MRE4 gene encodes a novel protein kinase homologue required for meiotic recombination in Saccharomyces cerevisiae. Nucl. Acids Res. 20:1992;449-457.
    • (1992) Nucl. Acids Res. , vol.20 , pp. 449-457
    • Leem, S.1    Ogawa, H.2
  • 14
    • 0033529330 scopus 로고    scopus 로고
    • Kinase interaction domain of kinase-associated protein phosphatase, a phosphoprotein-binding domain
    • Li J., Smith G. P., Walker J. C. Kinase interaction domain of kinase-associated protein phosphatase, a phosphoprotein-binding domain. Proc. Natl Acad. Sci. USA. 96:1999;7821-7826.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7821-7826
    • Li, J.1    Smith, G.P.2    Walker, J.C.3
  • 15
    • 0024362326 scopus 로고
    • Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: Application to interleukin 1 beta
    • Marion D., Driscoll P., Kay L., Wingfield P., Bax A., Gronenborn A., Clore G. Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta. Biochemistry. 28:1989;6150-6156.
    • (1989) Biochemistry , vol.28 , pp. 6150-6156
    • Marion, D.1    Driscoll, P.2    Kay, L.3    Wingfield, P.4    Bax, A.5    Gronenborn, A.6    Clore, G.7
  • 16
    • 0032484084 scopus 로고    scopus 로고
    • Linkage of ATM to cell cycle regulation by the Chk2 protein kinase
    • Matsuoka S., Huang M., Elledge S. Linkage of ATM to cell cycle regulation by the Chk2 protein kinase. Science. 282:1998;1893-1897.
    • (1998) Science , vol.282 , pp. 1893-1897
    • Matsuoka, S.1    Huang, M.2    Elledge, S.3
  • 17
    • 0028945424 scopus 로고
    • A kinase from fission yeast responsible for blocking mitosis in S phase
    • Murakami H., Okayama H. A kinase from fission yeast responsible for blocking mitosis in S phase. Nature. 374:1995;817-819.
    • (1995) Nature , vol.374 , pp. 817-819
    • Murakami, H.1    Okayama, H.2
  • 18
    • 0028979332 scopus 로고
    • DNA polymerase epsilon links the DNA replication machinery to the S phase checkpoint
    • Navas T., Zhou Z., Elledge S. DNA polymerase epsilon links the DNA replication machinery to the S phase checkpoint. Cell. 80:1995;29-39.
    • (1995) Cell , vol.80 , pp. 29-39
    • Navas, T.1    Zhou, Z.2    Elledge, S.3
  • 19
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding
    • Nilges M., Clore G., Gronenborn A. Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding. FEBS Letters. 239:1988;129-136.
    • (1988) FEBS Letters , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.2    Gronenborn, A.3
  • 20
    • 18844477320 scopus 로고    scopus 로고
    • A novel Drosophila nuclear protein serine/threonine kinase expressed in the germline during its establishment
    • Oishi I., Sugiyama S., Otani H., Yamamura H., Nishida Y., Minami Y. A novel Drosophila nuclear protein serine/threonine kinase expressed in the germline during its establishment. Mech. Dev. 71:1998;49-63.
    • (1998) Mech. Dev. , vol.71 , pp. 49-63
    • Oishi, I.1    Sugiyama, S.2    Otani, H.3    Yamamura, H.4    Nishida, Y.5    Minami, Y.6
  • 21
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson T., Scott J. Signaling through scaffold, anchoring, and adaptor proteins. Science. 278:1997;2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.2
  • 22
    • 0033518575 scopus 로고    scopus 로고
    • TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins
    • Salzmann M., Wider G., Pervushin K., Senn H., Wüthrich K. TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins. J. Am. Chem. Soc. 121:1999;844-848.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 844-848
    • Salzmann, M.1    Wider, G.2    Pervushin, K.3    Senn, H.4    Wüthrich, K.5
  • 23
    • 0027361196 scopus 로고
    • The cell proliferation-associated antigen of antibody Ki-67: A very large, ubiquitous nuclear protein with numerous repeated elements, representing a new kind of cell cycle-maintaining proteins
    • Schluter C., Duchrow M., Wohlenberg C., Becker M., Key G., Flad H., Gerdes J. The cell proliferation-associated antigen of antibody Ki-67: a very large, ubiquitous nuclear protein with numerous repeated elements, representing a new kind of cell cycle-maintaining proteins. J. Cell Biol. 123:1993;513-522.
    • (1993) J. Cell Biol. , vol.123 , pp. 513-522
    • Schluter, C.1    Duchrow, M.2    Wohlenberg, C.3    Becker, M.4    Key, G.5    Flad, H.6    Gerdes, J.7
  • 24
    • 0030837455 scopus 로고    scopus 로고
    • A structural basis for mutational inactivation of the tumour suppressor Smad4
    • Shi Y., Hata A., Lo R. S., Massague J., Pavletich N. P. A structural basis for mutational inactivation of the tumour suppressor Smad4. Nature. 388:1997;87-93.
    • (1997) Nature , vol.388 , pp. 87-93
    • Shi, Y.1    Hata, A.2    Lo, R.S.3    Massague, J.4    Pavletich, N.P.5
  • 26
    • 0028075896 scopus 로고
    • Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase
    • Stone J., Collinge M., Smith R., Horn M., Walker J. Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase. Science. 266:1994;793-795.
    • (1994) Science , vol.266 , pp. 793-795
    • Stone, J.1    Collinge, M.2    Smith, R.3    Horn, M.4    Walker, J.5
  • 27
    • 0032504069 scopus 로고    scopus 로고
    • Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint
    • Sun Z., Hsiao J., Fay D., Stern D. Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint. Science. 281:1998;272-274.
    • (1998) Science , vol.281 , pp. 272-274
    • Sun, Z.1    Hsiao, J.2    Fay, D.3    Stern, D.4
  • 28
    • 0032189952 scopus 로고    scopus 로고
    • The budding yeast Rad9 checkpoint protein is subjected to Mec1/Tel1-dependent hyperphosphorylation and interacts with Rad53 after DNA damage
    • Vialard J. E., Gilbert C. S., Green C. M., Lowndes N. F. The budding yeast Rad9 checkpoint protein is subjected to Mec1/Tel1-dependent hyperphosphorylation and interacts with Rad53 after DNA damage. EMBO J. 17:1998;5679-5688.
    • (1998) EMBO J. , vol.17 , pp. 5679-5688
    • Vialard, J.E.1    Gilbert, C.S.2    Green, C.M.3    Lowndes, N.F.4
  • 30
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner G., Braun W., Havel T., Schaumann T., Go N., Wuthrich K. Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196:1987;611-639.
    • (1987) J. Mol. Biol. , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.3    Schaumann, T.4    Go, N.5    Wuthrich, K.6
  • 32
    • 0021095743 scopus 로고
    • Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance
    • Wuthrich K., Billeter M., Braun W. Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J. Mol. Biol. 169:1983;949-961.
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wuthrich, K.1    Billeter, M.2    Braun, W.3
  • 34
    • 0027290933 scopus 로고
    • SPK1 is an essential S-phase-specific gene of Saccharomyces cerevisiae that encodes a nuclear serine/threonine/tyrosine kinase
    • Zheng P., Fay D., Burton J., Xiao H., Pinkham J., Stern D. SPK1 is an essential S-phase-specific gene of Saccharomyces cerevisiae that encodes a nuclear serine/threonine/tyrosine kinase. Mol. Cell. Biol. 13:1993;5829-5842.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5829-5842
    • Zheng, P.1    Fay, D.2    Burton, J.3    Xiao, H.4    Pinkham, J.5    Stern, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.