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Volumn 18, Issue 16, 1999, Pages 4438-4445

Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain

Author keywords

NMR spectroscopy; p53; SAM domain; Tumor suppressor

Indexed keywords

PROTEIN P73; PROTEIN TYROSINE KINASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0033575719     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.16.4438     Document Type: Article
Times cited : (154)

References (62)
  • 1
    • 0032569933 scopus 로고    scopus 로고
    • An insight into the life of p53: A protein coping with many functions! Review of the 9th p53 workshop, crete, May 9-13, 1998
    • Almog, N. and Rotter, V. (1998) An insight into the life of p53: a protein coping with many functions! Review of the 9th p53 Workshop, Crete, May 9-13, 1998. Biochim. Biophys. Acta, 1378, R43-R54.
    • (1998) Biochim. Biophys. Acta , vol.1378
    • Almog, N.1    Rotter, V.2
  • 2
    • 0031897589 scopus 로고    scopus 로고
    • Predicting functions from protein sequences - Where are the bottlenecks?
    • Bork, P. and Koonin, E.V. (1998) Predicting functions from protein sequences - where are the bottlenecks? Nature Genet., 18, 313-318.
    • (1998) Nature Genet. , vol.18 , pp. 313-318
    • Bork, P.1    Koonin, E.V.2
  • 5
    • 0033603494 scopus 로고    scopus 로고
    • p73 and p63 are homo-tetramers capable of weak hetero-typic interactions with each other but not with p53
    • Davison, T.D., Vagner, C., Kaghad, M., Ayed, A., Caput, D. and Arrowsmith, C.H. (1999) p73 and p63 are homo-tetramers capable of weak hetero-typic interactions with each other but not with p53. J. Biol. Chem., 274, 18709-18714.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18709-18714
    • Davison, T.D.1    Vagner, C.2    Kaghad, M.3    Ayed, A.4    Caput, D.5    Arrowsmith, C.H.6
  • 7
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX PIPES
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX PIPES. J. Biomol. NMR, 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 8
    • 0032516219 scopus 로고    scopus 로고
    • Human tumor-derived p53 proteins exhibit binding site selectivity and temperature sensitivity for transactivation in a yeast-based assay
    • Di Como, C.J. and Prives, C. (1998) Human tumor-derived p53 proteins exhibit binding site selectivity and temperature sensitivity for transactivation in a yeast-based assay. Oncogene, 16, 2527-2539.
    • (1998) Oncogene , vol.16 , pp. 2527-2539
    • Di Como, C.J.1    Prives, C.2
  • 9
    • 0032951530 scopus 로고    scopus 로고
    • p73 function is inhibited by tumor-derived p53 mutants in mammalian cells
    • Di Como, C.J., Gaiddon, C. and Prives, C. (1999) p73 function is inhibited by tumor-derived p53 mutants in mammalian cells. Mol. Cell. Biol., 19, 1438-1449.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1438-1449
    • Di Como, C.J.1    Gaiddon, C.2    Prives, C.3
  • 12
    • 0031110495 scopus 로고    scopus 로고
    • Floating stereospecific assignment revisited: Application to an 18kDa protein and comparison with J coupling data
    • Folmer, R., Hilbers, C., Konings, R. and Nilges, M. (1997) Floating stereospecific assignment revisited: application to an 18kDa protein and comparison with J coupling data. J. Biomol. NMR, 9, 245-258.
    • (1997) J. Biomol. NMR , vol.9 , pp. 245-258
    • Folmer, R.1    Hilbers, C.2    Konings, R.3    Nilges, M.4
  • 13
    • 0031473397 scopus 로고    scopus 로고
    • TEL gene rearrangements in myeloid malignancy
    • Golub, T.R. (1997) TEL gene rearrangements in myeloid malignancy. Hematol. Oncol. Clin. North Am., 11, 1207-1220.
    • (1997) Hematol. Oncol. Clin. North Am. , vol.11 , pp. 1207-1220
    • Golub, T.R.1
  • 14
    • 0028224348 scopus 로고
    • Fusion of PDGF receptor beta to a novel ets-like gene, tel, in chronic myelomonocytic leukemia with t(5;12) chromosomal translocation
    • Golub, T.R., Barker, G.F, Lovett, M. and Gilliland, D.G. (1994) Fusion of PDGF receptor beta to a novel ets-like gene, tel, in chronic myelomonocytic leukemia with t(5;12) chromosomal translocation. Cell, 77, 307-316.
    • (1994) Cell , vol.77 , pp. 307-316
    • Golub, T.R.1    Barker, G.F.2    Lovett, M.3    Gilliland, D.G.4
  • 15
    • 0030025773 scopus 로고    scopus 로고
    • Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours
    • Graeber, T.G., Osmanian, C., Jacks, T., Housman, D.E., Koch, C.J., Lowe, S.W. and Giaccia, A.J. (1996) Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours. Nature, 379, 88-91.
    • (1996) Nature , vol.379 , pp. 88-91
    • Graeber, T.G.1    Osmanian, C.2    Jacks, T.3    Housman, D.E.4    Koch, C.J.5    Lowe, S.W.6    Giaccia, A.J.7
  • 18
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 19
    • 0027991446 scopus 로고
    • The FSSP database of structurally aligned protein fold families
    • Holm, L. and Sander, C. (1994) The FSSP database of structurally aligned protein fold families. Nucleic Acids Res., 22, 3600-3609.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 20
    • 0026448672 scopus 로고
    • Regulation of the specific DNA binding function of p53
    • Hupp, T.R., Meek, D.W., Midgley, C.A. and Lane, D.P. (1992) Regulation of the specific DNA binding function of p53. Cell, 71, 875-886.
    • (1992) Cell , vol.71 , pp. 875-886
    • Hupp, T.R.1    Meek, D.W.2    Midgley, C.A.3    Lane, D.P.4
  • 21
    • 0029028352 scopus 로고
    • Mutational analysis of the carboxy-terminal portion of p53 using both yeast and mammalian cell assays in vivo
    • Ishioka, C., Englert, C., Winge, P., Yan, Y.-X., Engelstein, M. and Friend, S.H. (1995) Mutational analysis of the carboxy-terminal portion of p53 using both yeast and mammalian cell assays in vivo. Oncogene, 10, 1485-1492.
    • (1995) Oncogene , vol.10 , pp. 1485-1492
    • Ishioka, C.1    Englert, C.2    Winge, P.3    Yan, Y.-X.4    Engelstein, M.5    Friend, S.H.6
  • 22
    • 34249765651 scopus 로고
    • NMR VIEW - A computer program for the visualization and analysis of NMR data
    • Johnson, B.A. and Blevins, R.A. (1994) NMR VIEW - a computer program for the visualization and analysis of NMR Data. J. Biomol. NMR, 4, 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 23
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson, M.L., Correia, J.J., Yphantis, D.A. and Halvorson, H.R. (1981) Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys. J., 36, 575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 24
    • 0031564954 scopus 로고    scopus 로고
    • p73 is a human p53-related protein that can induce apoptosis
    • Jost, C.A., Marin, M.C. and Kaelin, W.G., Jr (1997) p73 is a human p53-related protein that can induce apoptosis. Nature, 389, 191-194.
    • (1997) Nature , vol.389 , pp. 191-194
    • Jost, C.A.1    Marin, M.C.2    Kaelin W.G., Jr.3
  • 25
    • 17144463437 scopus 로고    scopus 로고
    • A domain of TEL conserved in a subset of ETS proteins defines a specific oligomerization interface essential to the mitogenic properties of the TEL-PDGFR beta oncoprotein
    • Jousset, C. et al. (1997) A domain of TEL conserved in a subset of ETS proteins defines a specific oligomerization interface essential to the mitogenic properties of the TEL-PDGFR beta oncoprotein. EMBO J., 16, 69-82.
    • (1997) EMBO J. , vol.16 , pp. 69-82
    • Jousset, C.1
  • 26
    • 0030812331 scopus 로고    scopus 로고
    • Monoallelically expressed gene related to p53 at 1p36, a region frequently deleted in neuroblastoma and other cancers
    • Kaghad, M. et al. (1997) Monoallelically expressed gene related to p53 at 1p36, a region frequently deleted in neuroblastoma and other cancers. Cell, 90, 809-819.
    • (1997) Cell , vol.90 , pp. 809-819
    • Kaghad, M.1
  • 29
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L.E., Keifer, P. and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc., 114, 10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 31
    • 0029972806 scopus 로고    scopus 로고
    • p53: Puzzle and paradigm
    • Ko, L.J. and Prives, C. (1996) p53: puzzle and paradigm. Genes Dev., 10, 1054-1072.
    • (1996) Genes Dev. , vol.10 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 32
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 33
    • 0031938082 scopus 로고    scopus 로고
    • The SAM domain of polyhomeotic, RAE28 and scm mediates specific interactions through conserved residues
    • Kyba, M. and Brock, H.W. (1998) The SAM domain of polyhomeotic, RAE28 and scm mediates specific interactions through conserved residues. Dev. Genet., 22, 74-84.
    • (1998) Dev. Genet. , vol.22 , pp. 74-84
    • Kyba, M.1    Brock, H.W.2
  • 34
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R., Rullman, J., MacArthur, M., Kaptein, R. and Thornton, J. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR, 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.1    Rullman, J.2    MacArthur, M.3    Kaptein, R.4    Thornton, J.5
  • 35
    • 0027109075 scopus 로고
    • p53, guardian of the genome
    • Lane, D.P. (1992) p53, guardian of the genome. Nature, 358, 15-16.
    • (1992) Nature , vol.358 , pp. 15-16
    • Lane, D.P.1
  • 36
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine, A.J. (1997) p53, the cellular gatekeeper for growth and division. Cell, 88, 323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 37
    • 0025633582 scopus 로고
    • Germ line p53 mutations in a familial syndrome of breast cancer, sarcomas and other neoplasms
    • Malkin, D. et al. (1990) Germ line p53 mutations in a familial syndrome of breast cancer, sarcomas and other neoplasms. Science, 250, 1233-1238.
    • (1990) Science , vol.250 , pp. 1233-1238
    • Malkin, D.1
  • 38
    • 0028057108 scopus 로고
    • Raster 3D version 2.0. A program for realistic molecular graphics
    • Merritt, E.A. and Murphy, M.E. (1994) Raster 3D version 2.0. A program for realistic molecular graphics. Acta Crystallogr., D50, 869-873.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.2
  • 39
    • 0033594491 scopus 로고    scopus 로고
    • p63 is a p53 homologue required for limb and epidermal morphogenesis
    • Mills, A.A., Zheng, B., Wang, X.J., Vogel, H., Roop, D.R. and Bradley, A. (1999) p63 is a p53 homologue required for limb and epidermal morphogenesis. Nature, 398, 708-713.
    • (1999) Nature , vol.398 , pp. 708-713
    • Mills, A.A.1    Zheng, B.2    Wang, X.J.3    Vogel, H.4    Roop, D.R.5    Bradley, A.6
  • 40
    • 0029763189 scopus 로고    scopus 로고
    • Elongation factor TFIIS contains three structural domains: Solution structure of domain II
    • Morin, P.E., Awrey, D.E., Edwards, A.M. and Arrowsmith, C.H. (1996) Elongation factor TFIIS contains three structural domains: solution structure of domain II. Proc. Natl Acad. Sci. USA, 93, 10604-10608.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10604-10608
    • Morin, P.E.1    Awrey, D.E.2    Edwards, A.M.3    Arrowsmith, C.H.4
  • 41
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 42
    • 0028907436 scopus 로고
    • Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities
    • Nilges, M. (1995) Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities. J. Mol. Biol., 245, 645-660.
    • (1995) J. Mol. Biol. , vol.245 , pp. 645-660
    • Nilges, M.1
  • 43
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from β-spectrin
    • Nilges, M., Macias, M., O'Donoghue, S. and Oschkinat, H. (1997) Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from β-spectrin. J. Mol. Biol., 269, 408-422.
    • (1997) J. Mol. Biol. , vol.269 , pp. 408-422
    • Nilges, M.1    Macias, M.2    O'Donoghue, S.3    Oschkinat, H.4
  • 44
    • 0031852337 scopus 로고    scopus 로고
    • Cloning and functional analysis of human p51, which structurally and functionally resembles p53
    • Osada, M. et al. (1998) Cloning and functional analysis of human p51, which structurally and functionally resembles p53. Nature Med., 4, 839-843.
    • (1998) Nature Med. , vol.4 , pp. 839-843
    • Osada, M.1
  • 45
    • 0027771333 scopus 로고
    • The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spots
    • Pavletich, N.P., Chambers, K.A. and Pabo, C.O. (1993) The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spots. Genes Dev., 12, 2556-2564.
    • (1993) Genes Dev. , vol.12 , pp. 2556-2564
    • Pavletich, N.P.1    Chambers, K.A.2    Pabo, C.O.3
  • 46
    • 0030832045 scopus 로고    scopus 로고
    • A domain shared by the Polycomb group proteins scm and ph mediates heterotypic and homotypic interactions
    • Peterson, A.J., Kyba, M., Bornemann, D., Morgan, K., Brock, H.W. and Simon, J. (1997) A domain shared by the Polycomb group proteins Scm and ph mediates heterotypic and homotypic interactions. Mol. Cell. Biol., 17, 6683-6692.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6683-6692
    • Peterson, A.J.1    Kyba, M.2    Bornemann, D.3    Morgan, K.4    Brock, H.W.5    Simon, J.6
  • 47
    • 0025194489 scopus 로고
    • 1H NMR studies of human lysozyme: Spectral assignment and comparison with hen lysozyme
    • 1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme. Biochemistry, 29, 7201-7214.
    • (1990) Biochemistry , vol.29 , pp. 7201-7214
    • Redfield, C.1    Dobson, C.M.2
  • 49
    • 0030884751 scopus 로고    scopus 로고
    • A novel protein with strong homology to the tumor suppressor p53
    • Schmale, H. and Bamberger, C. (1997) A novel protein with strong homology to the tumor suppressor p53. Oncogene, 15, 1363-1367.
    • (1997) Oncogene , vol.15 , pp. 1363-1367
    • Schmale, H.1    Bamberger, C.2
  • 50
    • 0031022602 scopus 로고    scopus 로고
    • SAM as a protein interaction domain involved in developmental regulation
    • Schultz, J., Ponting, C.P., Hofmann, K. and Bork, P. (1997) SAM as a protein interaction domain involved in developmental regulation. Protein Sci., 6, 249-253.
    • (1997) Protein Sci. , vol.6 , pp. 249-253
    • Schultz, J.1    Ponting, C.P.2    Hofmann, K.3    Bork, P.4
  • 52
    • 0032881609 scopus 로고    scopus 로고
    • Solution structure of the receptor tyrosine kinase EphB2 SAM domain and identification of two distinct homotypic interaction sites
    • in press
    • Smalla, M., Schmieder, P., Kelly, M., terLaak, A., Krause, G., Ball, L., Wahl, M., Bork, P. and Oschkinat, H. (1999) Solution structure of the receptor tyrosine kinase EphB2 SAM domain and identification of two distinct homotypic interaction sites. Protein Sci., in press.
    • (1999) Protein Sci.
    • Smalla, M.1    Schmieder, P.2    Kelly, M.3    TerLaak, A.4    Krause, G.5    Ball, L.6    Wahl, M.7    Bork, P.8    Oschkinat, H.9
  • 54
    • 0032948019 scopus 로고    scopus 로고
    • The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization
    • Stapleton, D., Balan, I., Pawson, T. and Sicheri, F. (1999) The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization. Nature Struct. Biol., 6, 44-49.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 44-49
    • Stapleton, D.1    Balan, I.2    Pawson, T.3    Sicheri, F.4
  • 55
    • 0033524982 scopus 로고    scopus 로고
    • Oligomeric structure of the human EphB2 receptor SAM domain
    • Thanos, C.D., Goodwill, K.E. and Bowie, J.U. (1999) Oligomeric structure of the human EphB2 receptor SAM domain. Science, 283, 833-836.
    • (1999) Science , vol.283 , pp. 833-836
    • Thanos, C.D.1    Goodwill, K.E.2    Bowie, J.U.3
  • 57
    • 0027236269 scopus 로고
    • Interactions of human papillomavirus transforming proteins with the products of tumor suppressor genes
    • Vousden, K. (1993) Interactions of human papillomavirus transforming proteins with the products of tumor suppressor genes. FASEB J., 7, 872-879.
    • (1993) FASEB J. , vol.7 , pp. 872-879
    • Vousden, K.1
  • 58
    • 0024293423 scopus 로고
    • 1H nuclear magnetic resonance assignments from distance geometry calculations
    • 1H nuclear magnetic resonance assignments from distance geometry calculations. J. Mol. Biol., 204, 483-487.
    • (1988) J. Mol. Biol. , vol.204 , pp. 483-487
    • Weber, P.1    Morrison, A.2    Hare, D.3
  • 59
    • 0027244853 scopus 로고
    • The p53-mdm2 autoregulatory feedback loop
    • Wu, X., Bayle, J.H., Olson, D. and Levine, A.J. (1993) The p53-mdm2 autoregulatory feedback loop. Genes Dev., 7, 1126.
    • (1993) Genes Dev. , vol.7 , pp. 1126
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 60
    • 0032161624 scopus 로고    scopus 로고
    • p63, a p53 homolog at 3q27-29, encodes multiple products with transactivating, death-inducing and dominant-negative activities
    • Yang, A., Kaghad, M., Wang, Y., Gillett, E., Fleming, M.D., Dotsch, V., Andrews, N.C., Caput, D. and McKeon, F. (1998) p63, a p53 homolog at 3q27-29, encodes multiple products with transactivating, death-inducing and dominant-negative activities. Mol. Cell, 2, 305-316.
    • (1998) Mol. Cell , vol.2 , pp. 305-316
    • Yang, A.1    Kaghad, M.2    Wang, Y.3    Gillett, E.4    Fleming, M.D.5    Dotsch, V.6    Andrews, N.C.7    Caput, D.8    McKeon, F.9
  • 61
    • 0033594485 scopus 로고    scopus 로고
    • p63 is essential for regenerative proliferation in limb, craniofacial and epithelial development
    • Yang, A. et al. (1999) p63 is essential for regenerative proliferation in limb, craniofacial and epithelial development. Nature, 398, 714-718.
    • (1999) Nature , vol.398 , pp. 714-718
    • Yang, A.1
  • 62
    • 0032533514 scopus 로고    scopus 로고
    • The potential tumor suppressor p73 differentially regulates cellular p53 target genes
    • Zhu, J., Jiang, J., Zhou, W. and Chen, X. (1998) The potential tumor suppressor p73 differentially regulates cellular p53 target genes. Cancer Res., 58, 5061-5065.
    • (1998) Cancer Res. , vol.58 , pp. 5061-5065
    • Zhu, J.1    Jiang, J.2    Zhou, W.3    Chen, X.4


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