메뉴 건너뛰기




Volumn 4, Issue 3, 1997, Pages 231-238

Crystal structures of hint demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOTIDE BINDING PROTEIN;

EID: 0031051370     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0397-231     Document Type: Article
Times cited : (132)

References (54)
  • 1
    • 0027012508 scopus 로고
    • The HIT protein family: A new family of proteins present in prokaryotes yeast and mammals
    • Seraphin, B. The HIT protein family: a new family of proteins present in prokaryotes yeast and mammals. DNA Sequence 3, 177-179 (1992).
    • (1992) DNA Sequence , vol.3 , pp. 177-179
    • Seraphin, B.1
  • 2
    • 0026057757 scopus 로고
    • Characterization of a novel zinc binding site of protein kinase C inhbitor-1
    • Mozier, N.M., Walsh, M.P. & Pearson, J.D. Characterization of a novel zinc binding site of protein kinase C inhbitor-1. FEBS Lett. 279, 14-18 (1991).
    • (1991) FEBS Lett. , vol.279 , pp. 14-18
    • Mozier, N.M.1    Walsh, M.P.2    Pearson, J.D.3
  • 3
    • 0022273385 scopus 로고
    • Ca2+-binding proteins from bovine brain including a potent inhibitor of protein kinase C
    • McDonald, J.R. & Walsh, M.P. Ca2+-binding proteins from bovine brain including a potent inhibitor of protein kinase C. Biochem. J. 232, 559-567 (1985).
    • (1985) Biochem. J. , vol.232 , pp. 559-567
    • McDonald, J.R.1    Walsh, M.P.2
  • 4
    • 0029112667 scopus 로고
    • The product of the ataxia-telangiectasia group d complementing gene, atdc interacts with a protein kinase c substrate and inhibitor
    • Brzoska, P.M. et al. The product of the ataxia-telangiectasia group d complementing gene, atdc interacts with a protein kinase c substrate and inhibitor. Prac. Natl. Acad. Sci. USA 92, 7824-7828 (1995).
    • (1995) Prac. Natl. Acad. Sci. USA , vol.92 , pp. 7824-7828
    • Brzoska, P.M.1
  • 5
    • 0029980110 scopus 로고    scopus 로고
    • Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins
    • Lima, C., Klein, M.G., Weinstein, I.B. & Hendrickson, W.A. Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins. Proc. Natl. Acad. Sci. USA 93, 5357-5362 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5357-5362
    • Lima, C.1    Klein, M.G.2    Weinstein, I.B.3    Hendrickson, W.A.4
  • 6
    • 0030586910 scopus 로고    scopus 로고
    • Cloning, mapping, and in vivo localization of a human member of the PKCI-1 protein family (PRKCNH1)
    • Brzoska, P.M. et al. Cloning, mapping, and in vivo localization of a human member of the PKCI-1 protein family (PRKCNH1).Genomics 36, 151-156 (1996).
    • (1996) Genomics , vol.36 , pp. 151-156
    • Brzoska, P.M.1
  • 7
    • 0028238262 scopus 로고
    • Isolation of a maize cDNa encoding a protein with extensive similarity to an inhibitor of protein kinase C and a cyanobacterial open reading frame
    • Simpson, G.G., Clark, G. & Brown, J.W. Isolation of a maize cDNA encoding a protein with extensive similarity to an inhibitor of protein kinase C and a cyanobacterial open reading frame. Biochem. Biophys. Acta 1222, 306-308 (1994).
    • (1994) Biochem. Biophys. Acta , vol.1222 , pp. 306-308
    • Simpson, G.G.1    Clark, G.2    Brown, J.W.3
  • 8
    • 0028295681 scopus 로고
    • 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans
    • Wilson, R. et al. 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature 368, 32-38 (1994).
    • (1994) Nature , vol.368 , pp. 32-38
    • Wilson, R.1
  • 9
    • 0025913947 scopus 로고
    • Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression
    • Frohlich, K.U. et al. Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression. J. Cell Biol. 114, 443-453 (1991).
    • (1991) J. Cell Biol. , vol.114 , pp. 443-453
    • Frohlich, K.U.1
  • 10
    • 0025344505 scopus 로고
    • Different and rapid responses of four cyanobacterial psbA transcripts to changes in light intensity
    • Bustos, S.A., Schaefer, M.R. & Golden, S.S. Different and rapid responses of four cyanobacterial psbA transcripts to changes in light intensity. J. Bacteriol. 172, 1998-2004 (1990).
    • (1990) J. Bacteriol. , vol.172 , pp. 1998-2004
    • Bustos, S.A.1    Schaefer, M.R.2    Golden, S.S.3
  • 11
    • 0029653518 scopus 로고
    • Whole-genome random sequencing and assembly of Haemophilus influenzae Rd
    • Fleischmann, R.D. et al. Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269, 496-512 (1995).
    • (1995) Science , vol.269 , pp. 496-512
    • Fleischmann, R.D.1
  • 12
    • 0024652298 scopus 로고
    • Cloning of histidine genes of Azospirillum brasilense: Organization of the ABFH gene cluster and nucleotide sequence of the hisB gene
    • Fani, R. et al. Cloning of histidine genes of Azospirillum brasilense: organization of the ABFH gene cluster and nucleotide sequence of the hisB gene. Mol. Gen. Genet. 216, 224-229 (1989).
    • (1989) Mol. Gen. Genet. , vol.216 , pp. 224-229
    • Fani, R.1
  • 13
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bult, C.J. et al. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273, 1058-1073 (1996).
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1
  • 14
    • 0028829125 scopus 로고
    • The minimal gene complement of Mycoplasma genitalium
    • Fraser, C.M. et al. The minimal gene complement of Mycoplasma genitalium. Science 270, 397-403 (1995).
    • (1995) Science , vol.270 , pp. 397-403
    • Fraser, C.M.1
  • 15
    • 13344279424 scopus 로고    scopus 로고
    • The FHIT gene, spanning the chromosome 3p14.2 fragile site and renal carcinoma-associated t(3;8) breakpoint, is abnormal in digestive tract cancers
    • Ohta, M. et al. The FHIT gene, spanning the chromosome 3p14.2 fragile site and renal carcinoma-associated t(3;8) breakpoint, is abnormal in digestive tract cancers. Cell 84, 587-597 (1996).
    • (1996) Cell , vol.84 , pp. 587-597
    • Ohta, M.1
  • 16
    • 0029562527 scopus 로고
    • Cloning of the Schizosaccharomyces pombe gene encoding diadenosine 5′,5-P1,P4-tetraphosphate (Ap4A) asymmetrical hydrolase: Sequence similarity with the histidine triad (HIT) protein family
    • Huang, Y., Garrison, P.N. & Barnes, L.D. Cloning of the Schizosaccharomyces pombe gene encoding diadenosine 5′,5-P1,P4-tetraphosphate (Ap4A) asymmetrical hydrolase: sequence similarity with the histidine triad (HIT) protein family. Biochem. J. 312, 925-932 (1995).
    • (1995) Biochem. J. , vol.312 , pp. 925-932
    • Huang, Y.1    Garrison, P.N.2    Barnes, L.D.3
  • 17
    • 0029840316 scopus 로고    scopus 로고
    • FHIT, a putative tumor suppressor in humans, is a dinucleoside 5′,5‴-P-1,P-3-triphosphate hydrolase
    • Barnes, L.D. et al. FHIT, a putative tumor suppressor in humans, is a dinucleoside 5′,5‴-P-1,P-3-triphosphate hydrolase. Biochemistry 35, 11529-11535 (1996).
    • (1996) Biochemistry , vol.35 , pp. 11529-11535
    • Barnes, L.D.1
  • 19
    • 15844384990 scopus 로고    scopus 로고
    • The FHIT gene at 3p14.2 is abnormal in lung cancer
    • Sozzi, G. et al. The FHIT gene at 3p14.2 is abnormal in lung cancer. Cell 85, 17-26 (1996).
    • (1996) Cell , vol.85 , pp. 17-26
    • Sozzi, G.1
  • 20
    • 9344225158 scopus 로고    scopus 로고
    • Aberrant FHIT transcripts in Merkel cell carcinoma
    • Sozzi, G. et al. Aberrant FHIT transcripts in Merkel cell carcinoma. Cancer Research 56, 2472-2474 (1996).
    • (1996) Cancer Research , vol.56 , pp. 2472-2474
    • Sozzi, G.1
  • 21
    • 0029902071 scopus 로고    scopus 로고
    • The FHIT gene at 3p14.2 is abnormal in breast carcinomas
    • Negrini, M. et al. The FHIT gene at 3p14.2 is abnormal in breast carcinomas. Cancer Research 56, 3173-3179 (1996).
    • (1996) Cancer Research , vol.56 , pp. 3173-3179
    • Negrini, M.1
  • 22
    • 0029795913 scopus 로고    scopus 로고
    • FHIT gene alterations in head and neck squamous cell carcinomas
    • Virgilio, L. et al. FHIT gene alterations in head and neck squamous cell carcinomas. Proc. Natl. Acad. Sci. USA 93, 9770-9775 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9770-9775
    • Virgilio, L.1
  • 23
    • 10144234126 scopus 로고    scopus 로고
    • Frequent breakpoints in the 3p14.2 fragile site, Fra3b, in pancreatic tumors
    • Shridhar, R. et al. Frequent breakpoints in the 3p14.2 fragile site, Fra3b, in pancreatic tumors. Cancer Research 56, 4347-4350 (1996).
    • (1996) Cancer Research , vol.56 , pp. 4347-4350
    • Shridhar, R.1
  • 24
    • 0029903698 scopus 로고    scopus 로고
    • The FHIT and PTPRG genes are deleted in benign proliferative breast disease associated with familial breast cancer and cytogenetic rearrangements of chromosome band 3p14
    • Panagopoulos, I. et al. The FHIT and PTPRG genes are deleted in benign proliferative breast disease associated with familial breast cancer and cytogenetic rearrangements of chromosome band 3p14. Cancer Research 56, 4871-4875 (1996).
    • (1996) Cancer Research , vol.56 , pp. 4871-4875
    • Panagopoulos, I.1
  • 25
    • 0029830791 scopus 로고    scopus 로고
    • Frequent abnormalities of fhit, a candidate tumor suppressor gene, in head and neck cancer cell lines
    • Mao, L., Fan, Y.H., Lotan, R. & Hong, W.K. Frequent abnormalities of fhit, a candidate tumor suppressor gene, in head and neck cancer cell lines. Cancer Research 56, 5128-5131 (1996).
    • (1996) Cancer Research , vol.56 , pp. 5128-5131
    • Mao, L.1    Fan, Y.H.2    Lotan, R.3    Hong, W.K.4
  • 26
    • 0030461143 scopus 로고    scopus 로고
    • High levels of allele loss at the FHIT and ATM genes in non-comedo ductal carcinoma in situ and grade I tubular invasive breast cancers
    • Man, S., Ellis, I.O., Sibbering, M., Blamey, R.W. & Brook, J.D. High levels of allele loss at the FHIT and ATM genes in non-comedo ductal carcinoma in situ and grade I tubular invasive breast cancers. Cancer Research 56, 5484-5489 (1996).
    • (1996) Cancer Research , vol.56 , pp. 5484-5489
    • Man, S.1    Ellis, I.O.2    Sibbering, M.3    Blamey, R.W.4    Brook, J.D.5
  • 27
    • 0029731629 scopus 로고    scopus 로고
    • Molecular analysis of the FHIT gene at 3p14.2 in lung cancer cell lines
    • Yanagisawa, K. et al. Molecular analysis of the FHIT gene at 3p14.2 in lung cancer cell lines. Cancer Research 56, 5579-5582 (1996).
    • (1996) Cancer Research , vol.56 , pp. 5579-5582
    • Yanagisawa, K.1
  • 28
    • 0031013993 scopus 로고    scopus 로고
    • Expression of reciprocal hybrid transcripts of HMGIC and FHIT in a pleomorphic adenoma of the parotid gland
    • Geurts, J.M.W., Schoenmakers, E.F.P.M., Roijer, E., Stenman, G. & Van de Ven, W.J.M. Expression of reciprocal hybrid transcripts of HMGIC and FHIT in a pleomorphic adenoma of the parotid gland. Cancer Research 57, 13-17 (1997).
    • (1997) Cancer Research , vol.57 , pp. 13-17
    • Geurts, J.M.W.1    Schoenmakers, E.F.P.M.2    Roijer, E.3    Stenman, G.4    Van De Ven, W.J.M.5
  • 29
    • 0029113143 scopus 로고
    • Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 Å resolution
    • Wedekind, J.E., Frey, P.A. & Rayment, I. Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 Å resolution. Biochemistry 34, 11049-11061 (1995).
    • (1995) Biochemistry , vol.34 , pp. 11049-11061
    • Wedekind, J.E.1    Frey, P.A.2    Rayment, I.3
  • 30
    • 0018178756 scopus 로고
    • Newborn screening for galactosemia and other galactose metabolic defects
    • Levy, H.L. & Hammersen, G. Newborn screening for galactosemia and other galactose metabolic defects. J. Pediatr. 92, 871-877 (1978).
    • (1978) J. Pediatr. , vol.92 , pp. 871-877
    • Levy, H.L.1    Hammersen, G.2
  • 32
    • 0025814761 scopus 로고
    • Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein
    • Rosen, M.K., Michnick, S.W., Karplus, M. & Schreiber, S.L. Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein. Biochemistry 30, 4774-4789 (1991).
    • (1991) Biochemistry , vol.30 , pp. 4774-4789
    • Rosen, M.K.1    Michnick, S.W.2    Karplus, M.3    Schreiber, S.L.4
  • 33
    • 0025826966 scopus 로고
    • Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin
    • Michnick, S.W., Rosen, M.K., Wandless, T.J., Karplus, M. & Schreiber, S.L. Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin. Science 252, 836-839 (1991).
    • (1991) Science , vol.252 , pp. 836-839
    • Michnick, S.W.1    Rosen, M.K.2    Wandless, T.J.3    Karplus, M.4    Schreiber, S.L.5
  • 34
    • 0025728258 scopus 로고
    • Solution structure of the major binding protein for the immunosuppressant FK506
    • Moore, J.M., Peattie, D.A., Fitzgibbon, M.J. & Thomson, J.A. Solution structure of the major binding protein for the immunosuppressant FK506. Nature 351, 248-250 (1991).
    • (1991) Nature , vol.351 , pp. 248-250
    • Moore, J.M.1    Peattie, D.A.2    Fitzgibbon, M.J.3    Thomson, J.A.4
  • 35
    • 0000838678 scopus 로고
    • Comparitive X-ray Structures of the Major Binding Protein for the Immunosuppressant FK506 (Tacrolimus) in Unliganded Form and in Complex with FK506 and Rapamycin
    • Wilson, K.P. et al. Comparitive X-ray Structures of the Major Binding Protein for the Immunosuppressant FK506 (Tacrolimus) in Unliganded Form and in Complex with FK506 and Rapamycin. Acta Crystallogr. D 51, 511-521 (1995).
    • (1995) Acta Crystallogr. D , vol.51 , pp. 511-521
    • Wilson, K.P.1
  • 36
    • 0028928611 scopus 로고
    • The chemistry of signal transduction
    • Clardy, J. The chemistry of signal transduction. Proc. Natl. Acad. Sci. USA 92, 56-61 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 56-61
    • Clardy, J.1
  • 37
    • 0001956114 scopus 로고
    • Enzymes cleaving dinucleoside polyphosphates
    • (ed. McLennan, A.G.) CRC Press, Boca Raton, FL
    • Guranowski, A. & Sillero, A. Enzymes cleaving dinucleoside polyphosphates. in Ap4A and Other Dinucleoside Polyphosphates (ed. McLennan, A.G.) 81-133 (CRC Press, Boca Raton, FL, 1992).
    • (1992) Ap4A and Other Dinucleoside Polyphosphates , pp. 81-133
    • Guranowski, A.1    Sillero, A.2
  • 38
    • 0029102896 scopus 로고
    • An alleged yeast polyphosphate kinase is actually diadenosine-5′, 5″′-P1,P4-tetraphosphate alpha, beta-phosphorylase
    • Booth, J.W. & Guidotti, G. An alleged yeast polyphosphate kinase is actually diadenosine-5′, 5″′-P1,P4-tetraphosphate alpha, beta-phosphorylase. J. Biol. Chem. 270, 19377-19382 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 19377-19382
    • Booth, J.W.1    Guidotti, G.2
  • 39
    • 0029810819 scopus 로고    scopus 로고
    • The structure of nucleotidylated Histidine-166 of Galactose-1-Phosphate Uridylyltransferase provides insight into phosphoryl group transfer
    • Wedekind, J.E., Frey, P.A. & Rayment, I. The structure of nucleotidylated Histidine-166 of Galactose-1-Phosphate Uridylyltransferase provides insight into phosphoryl group transfer. Biochemistry 35, 11560-11569 (1996).
    • (1996) Biochemistry , vol.35 , pp. 11560-11569
    • Wedekind, J.E.1    Frey, P.A.2    Rayment, I.3
  • 40
    • 0027457235 scopus 로고
    • Isolation and characterization of diadenosine tetraphosphate (Ap4A) hydrolase from Schizosaccharomyces pombe
    • Robinson, A.K., de la Pena, C.E. & Barnes, L.D. Isolation and characterization of diadenosine tetraphosphate (Ap4A) hydrolase from Schizosaccharomyces pombe. Biochemica et Biophysica Acta 1161, 139-148 (1993).
    • (1993) Biochemica et Biophysica Acta , vol.1161 , pp. 139-148
    • Robinson, A.K.1    De La Pena, C.E.2    Barnes, L.D.3
  • 42
    • 0030030155 scopus 로고    scopus 로고
    • Interferons induce accumulation of diadenosine triphosphate (Ap3A) in human cultured cells
    • Vartanian, A., Narovlyansky, A., Amchenkova, A., Turpaev, K. & Kisselev, L. Interferons induce accumulation of diadenosine triphosphate (Ap3A) in human cultured cells. FEBS Lett. 381, 32-34 (1996).
    • (1996) FEBS Lett. , vol.381 , pp. 32-34
    • Vartanian, A.1    Narovlyansky, A.2    Amchenkova, A.3    Turpaev, K.4    Kisselev, L.5
  • 43
    • 0023039248 scopus 로고
    • Relationship between cellular diadenosine 5′,5‴-P1,P4-tetraphosphate level, cell density, cell growth stimulation and toxic stresses
    • Segal, E. & Le Pecq, J.B. Relationship between cellular diadenosine 5′,5‴-P1,P4-tetraphosphate level, cell density, cell growth stimulation and toxic stresses. Exp. Cell Res. 167, 119-126 (1986).
    • (1986) Exp. Cell Res. , vol.167 , pp. 119-126
    • Segal, E.1    Le Pecq, J.B.2
  • 44
    • 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, 795-800 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 46
    • 0016872966 scopus 로고
    • Three-dimensional Fourier Synthesis of Human Deoxyhemoglobin at 2.5 Angstrom Resolution
    • Ten Eyck, L.F. & Arnone, A. Three-dimensional Fourier Synthesis of Human Deoxyhemoglobin at 2.5 Angstrom Resolution. J. Mol. Biol. 100, 3-11 (1976).
    • (1976) J. Mol. Biol. , vol.100 , pp. 3-11
    • Ten Eyck, L.F.1    Arnone, A.2
  • 47
    • 0022325950 scopus 로고
    • Resolution of phase ambiguity in macromolecular crystallography
    • Wang, B.C. Resolution of phase ambiguity in macromolecular crystallography. Methods Enzymol. 115, 90-112 (1985).
    • (1985) Methods Enzymol. , vol.115 , pp. 90-112
    • Wang, B.C.1
  • 48
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 51
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. D 50, 157-163 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 157-163
    • Navaza, J.1
  • 52
    • 16044370755 scopus 로고    scopus 로고
    • The free R value: A more objective statistic for crystallography
    • in press
    • Brunger, A.T. The free R value: a more objective statistic for crystallography. Methods in Enzymol. 277, in press (1997).
    • (1997) Methods in Enzymol. , vol.277
    • Brunger, A.T.1
  • 53
    • 0027412196 scopus 로고
    • ALSCRIPT, a tool to format multiple sequence alignments
    • Barton, G.J. ALSCRIPT, a tool to format multiple sequence alignments. Protein Engineering 6, 37-40 (1993).
    • (1993) Protein Engineering , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 54
    • 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, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.