메뉴 건너뛰기




Volumn 57, Issue 5, 2000, Pages 851-858

Three-dimensional model of human TIP30, a coactivator for HIV-1 Tat-activated transcription, and CC3, a protein associated with metastasis suppression

Author keywords

CC3; HIV 1; Metastasis; Tat; TIP30

Indexed keywords

CC30; LYSINE; OXIDOREDUCTASE; SERINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 0034045656     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050047     Document Type: Article
Times cited : (28)

References (36)
  • 1
    • 0032478173 scopus 로고    scopus 로고
    • A cofactor, TIP30. Specifically enhances HIV-1 Tat-activated transcription
    • 1 Xiao H., Tao Y., Greenblutt J. and Roeder R. G. (1998) A cofactor, TIP30. specifically enhances HIV-1 Tat-activated transcription. Proc. Natl. Acad. Sci. USA 95: 2146-2151
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2146-2151
    • Xiao, H.1    Tao, Y.2    Greenblutt, J.3    Roeder, R.G.4
  • 2
    • 0030996563 scopus 로고    scopus 로고
    • A link between metastasis and resistance to apoptosis of variant small cell lung carcinoma
    • 2 Shtivelman E. (1997) A link between metastasis and resistance to apoptosis of variant small cell lung carcinoma. Oncogene 14: 2167-2173
    • (1997) Oncogene , vol.14 , pp. 2167-2173
    • Shtivelman, E.1
  • 3
    • 0033166792 scopus 로고    scopus 로고
    • TIP30, a cofactor for HIV-I Tat-activated transcription, is homologous to short-chain dehydrogenases/reductases
    • 3 Baker M. E. (1999) TIP30, a cofactor for HIV-I Tat-activated transcription, is homologous to short-chain dehydrogenases/reductases. Curr. Biol. 9: R471
    • (1999) Curr. Biol. , vol.9
    • Baker, M.E.1
  • 5
    • 0026828603 scopus 로고
    • 11β-Hydroxysteroid dehydrogenase and the short chain alcohol dehydrogenase (SCAD) superfamily
    • 5 Krozowski Z. (1992) 11β-Hydroxysteroid dehydrogenase and the short chain alcohol dehydrogenase (SCAD) superfamily. Mol. Cell. Endocrinol. 84: C25-C31
    • (1992) Mol. Cell. Endocrinol. , vol.84
    • Krozowski, Z.1
  • 6
    • 0030784438 scopus 로고    scopus 로고
    • An artificial intelligence approach to motif discovery in protein sequences: Application to steroid dehydrogenases
    • 6 Bailey T. L., Baker M. E. and Elkan C. P. (1997) An artificial intelligence approach to motif discovery in protein sequences: application to steroid dehydrogenases. J. Steroid Biochem. Mol. Biol. 62: 29-43
    • (1997) J. Steroid Biochem. Mol. Biol. , vol.62 , pp. 29-43
    • Bailey, T.L.1    Baker, M.E.2    Elkan, C.P.3
  • 7
    • 0025883535 scopus 로고
    • Characteristics of short-chain alcohol dehydrogenase related enzymes
    • 7 Persson B., Krook M. and Jornvall H. (1991) Characteristics of short-chain alcohol dehydrogenase related enzymes. Eur. J. Biochem. 200: 537-543
    • (1991) Eur. J. Biochem. , vol.200 , pp. 537-543
    • Persson, B.1    Krook, M.2    Jornvall, H.3
  • 9
    • 0028773893 scopus 로고
    • The refined three-dimensional structure of 3α,20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in chart-chain dehydrogenases
    • 9 Ghosh D., Wawrzak Z., Weeks C. M., Duax W. L. and Erman M. (1994) The refined three-dimensional structure of 3α,20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in chart-chain dehydrogenases. Structure 2: 629-640
    • (1994) Structure , vol.2 , pp. 629-640
    • Ghosh, D.1    Wawrzak, Z.2    Weeks, C.M.3    Duax, W.L.4    Erman, M.5
  • 10
    • 0030000879 scopus 로고    scopus 로고
    • Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from Escherichia coli
    • 10 Tanaka N., Nonaka T., Tanabe T., Yoshimoto T., Tsuru D. and Mitsui Y. (1996) Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from Escherichia coli. Biochemistry 35: 7715-7730
    • (1996) Biochemistry , vol.35 , pp. 7715-7730
    • Tanaka, N.1    Nonaka, T.2    Tanabe, T.3    Yoshimoto, T.4    Tsuru, D.5    Mitsui, Y.6
  • 11
    • 0029877040 scopus 로고    scopus 로고
    • Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli
    • 11 Thoden J. B., Frey P. A. and Holden H. M. (1996) Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli. Biochemistry 35: 2557-2566
    • (1996) Biochemistry , vol.35 , pp. 2557-2566
    • Thoden, J.B.1    Frey, P.A.2    Holden, H.M.3
  • 13
    • 0028331213 scopus 로고
    • Sequence analysis of steroid-and prostaglandin-metabolizing enzymes: Application to understanding catalysis
    • 13 Baker M. E. (1994) Sequence analysis of steroid-and prostaglandin-metabolizing enzymes: application to understanding catalysis. Steroids 59: 248-258
    • (1994) Steroids , vol.59 , pp. 248-258
    • Baker, M.E.1
  • 14
    • 0026445622 scopus 로고
    • Tyr-179 and Lys-183 are essential for enzymatic activity of 11β-hydroxysteroid dehydrogenase
    • 14 Obeid J. and White P. C. (1992) Tyr-179 and Lys-183 are essential for enzymatic activity of 11β-hydroxysteroid dehydrogenase. Biochem. Biophys. Res. Commun. 188: 222-227
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 222-227
    • Obeid, J.1    White, P.C.2
  • 15
    • 0027309435 scopus 로고
    • Site-specific mutagenesis of Drosophila alcohol dehydrogenase: Evidence for involvement of tyrosine-152 and lysine-156 in catalysis
    • 15 Chen Z., Jiang J. C., Lin Z. G., Lee W. R., Baker M. E. and Chang S. H. (1993) Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis. Biochemistry 32: 3342-3346
    • (1993) Biochemistry , vol.32 , pp. 3342-3346
    • Chen, Z.1    Jiang, J.C.2    Lin, Z.G.3    Lee, W.R.4    Baker, M.E.5    Chang, S.H.6
  • 16
    • 0029561114 scopus 로고
    • Structures important in mammalian 11β and 17β-hydroxysteroid dehydrogenases
    • 16 Tsigelny I. and Baker M. E. (1995) Structures important in mammalian 11β and 17β-hydroxysteroid dehydrogenases. J. Ster. Biochem. Mol. Biol. 55: 589-600
    • (1995) J. Ster. Biochem. Mol. Biol. , vol.55 , pp. 589-600
    • Tsigelny, I.1    Baker, M.E.2
  • 17
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • 17 Chothia C. and Lesk A. M. (1986) The relation between the divergence of sequence and structure in proteins. EMBO J. 5: 823-826
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 19
    • 0009130599 scopus 로고    scopus 로고
    • A structural explanation for the twilight zone of protein sequence homology
    • 19 Chung S. Y. and Subbiah S. (1996) A structural explanation for the twilight zone of protein sequence homology. Structure 4: 1123-1127
    • (1996) Structure , vol.4 , pp. 1123-1127
    • Chung, S.Y.1    Subbiah, S.2
  • 20
    • 0026521505 scopus 로고
    • Expansion of the mammalian 3β-hydroxysteroid dehydrogenase/plant dihydroflavonol reductase superfamily to include a bacterial cholesterol dehhydrogenase, a bacterial UDP-galactose-4-cpimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus
    • 20 Baker M. E. and Blasco R. (1992) Expansion of the mammalian 3β-hydroxysteroid dehydrogenase/plant dihydroflavonol reductase superfamily to include a bacterial cholesterol dehhydrogenase, a bacterial UDP-galactose-4-cpimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus. FEBS Lett. 301: 89-93
    • (1992) FEBS Lett. , vol.301 , pp. 89-93
    • Baker, M.E.1    Blasco, R.2
  • 21
    • 0032898876 scopus 로고    scopus 로고
    • A common ancestor for a subunit in the mitochondrial proton-translocating NADH:Ubiquinone oxidoreductase (complex I) and short-chain dehydrogenases reductases
    • 21 Baker M. E., Grundy W. N. and Elkan C. P. (1999) A common ancestor for a subunit in the mitochondrial proton-translocating NADH:ubiquinone oxidoreductase (complex I) and short-chain dehydrogenases reductases. Cell. Mol. Life Sci. 55: 450-455
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 450-455
    • Baker, M.E.1    Grundy, W.N.2    Elkan, C.P.3
  • 22
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • 22 Sali A. and Blundell T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234: 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 24
    • 0029643855 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: The structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family
    • 24 Tanaka N., Nonaka T., Nakanishi M., Deyashiki Y., Hara A. and Mitsui Y. (1996) Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family. Structure 4: 33-45
    • (1996) Structure , vol.4 , pp. 33-45
    • Tanaka, N.1    Nonaka, T.2    Nakanishi, M.3    Deyashiki, Y.4    Hara, A.5    Mitsui, Y.6
  • 25
    • 0017868338 scopus 로고
    • Empirical predications of protein structure
    • 25 Chou P. Y. and Fasman G. D. (1978) Empirical predications of protein structure. Annu. Rev. Biochem. 47: 251-276
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 26
    • 0023555768 scopus 로고
    • Further developments of protein secondary structure prediction using information theory: New parameters and consideration of residue pairs
    • 26 Gibrat J. F., Garnier J. and Robson B. (1987) Further developments of protein secondary structure prediction using information theory: new parameters and consideration of residue pairs. J. Mol. Biol. 198: 425-443
    • (1987) J. Mol. Biol. , vol.198 , pp. 425-443
    • Gibrat, J.F.1    Garnier, J.2    Robson, B.3
  • 27
    • 33845318295 scopus 로고
    • Interaction of pyrophosphate moieties with α-helixes in dinucleotide binding proteins
    • 27 Wierenga R. K., De Maeyer M. C. and Hol W. G. J. (1985) Interaction of pyrophosphate moieties with α-helixes in dinucleotide binding proteins. Biochemistry 24: 1346-1357
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.K.1    De Maeyer, M.C.2    Hol, W.G.J.3
  • 28
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins using an amino acid sequence fingerprint
    • 28 Wierenga R. K., Terpstra P. P. and Hol W. G. J. (1986) Prediction of the occurrence of the ADP-binding βαβ-fold in proteins using an amino acid sequence fingerprint. J. Mol. Biol. 187: 101-107
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.P.2    Hol, W.G.J.3
  • 30
    • 0031035010 scopus 로고    scopus 로고
    • Switch of coenzyme specificity of mouse lung carbonyl reductase by substitution of threonine 38 with aspartic acid
    • 30 Nakanishi M., Matsuura K., Kaibe H., Tanaka N., Nonaka T., Mitsui Y. et al. (1997) Switch of coenzyme specificity of mouse lung carbonyl reductase by substitution of threonine 38 with aspartic acid. J. Biol. Chem. 272: 2218-2222
    • (1997) J. Biol. Chem. , vol.272 , pp. 2218-2222
    • Nakanishi, M.1    Matsuura, K.2    Kaibe, H.3    Tanaka, N.4    Nonaka, T.5    Mitsui, Y.6
  • 32
    • 0029619241 scopus 로고
    • Structures stabilizing the dimer interface on human 11β-hydroxysteroid dehydrogenase-types 1 and 2 and human 15-hydroxyprostaglandin dehydrogenase and their homologs
    • 32 Tsigelny I. and Baker M. E. (1995) Structures stabilizing the dimer interface on human 11β-hydroxysteroid dehydrogenase-types 1 and 2 and human 15-hydroxyprostaglandin dehydrogenase and their homologs. Biochem. Biophys. Res. Commun. 217: 859-868
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 859-868
    • Tsigelny, I.1    Baker, M.E.2
  • 33
    • 0032544367 scopus 로고    scopus 로고
    • The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 Å resolution
    • 33 Benach J., Atrian S., Gonzalez-Duarte R. and Ladenstein R. (1998) The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 Å resolution. J. Mol. Biol. 282: 383-399
    • (1998) J. Mol. Biol. , vol.282 , pp. 383-399
    • Benach, J.1    Atrian, S.2    Gonzalez-Duarte, R.3    Ladenstein, R.4
  • 34
    • 0029039935 scopus 로고
    • Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase
    • 34 Chenevert S. W., Fossett N. G., Chang S. H., Tsigelny I., Baker M. E. and Lee W. R. (1995) Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase. Biochem. J. 308: 419-423
    • (1995) Biochem. J. , vol.308 , pp. 419-423
    • Chenevert, S.W.1    Fossett, N.G.2    Chang, S.H.3    Tsigelny, I.4    Baker, M.E.5    Lee, W.R.6
  • 35
    • 0019495032 scopus 로고
    • Purification and properties of an NADPH-dependent carbonyl reductase from human brain: Relationship to prostaglandin 9-keto reductase and xenobiotic ketone reductase
    • 35 Wermuth B. (1981) Purification and properties of an NADPH-dependent carbonyl reductase from human brain: relationship to prostaglandin 9-keto reductase and xenobiotic ketone reductase. J. Biol. Chem. 256: 1206-1213
    • (1981) J. Biol. Chem. , vol.256 , pp. 1206-1213
    • Wermuth, B.1
  • 36
    • 0026681607 scopus 로고
    • Pig testicular 20 beta-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity: cDNA cloning of pig testicular 20 beta-hydroxysteroid dehydrogenase
    • 36 Tanaka M., Ohno S., Adachi S., Nakajin S., Shinoda M. and Nagahama Y. (1992) Pig testicular 20 beta-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity: cDNA cloning of pig testicular 20 beta-hydroxysteroid dehydrogenase. J. Biol. Chem. 267: 13451-13455
    • (1992) J. Biol. Chem. , vol.267 , pp. 13451-13455
    • Tanaka, M.1    Ohno, S.2    Adachi, S.3    Nakajin, S.4    Shinoda, M.5    Nagahama, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.