메뉴 건너뛰기




Volumn 16, Issue 12, 1997, Pages 3396-3404

Stucture of the PH domain and Btk motif from Bruton's tyrosine kinase: Molecular explanations for X-linked agammaglobulinaemia

Author keywords

Bruton's tyrosine kinase; Btk motif; Inositol phosphates; PH domain; X linked agammaglobulinaemia

Indexed keywords

CYSTEINE; HISTIDINE; INOSITOL PHOSPHATE; LIPID BINDING PROTEIN; PHOSPHATIDYLINOSITOL; PLECKSTRIN; PROTEIN TYROSINE KINASE; ZINC; AGAMMAGLOBULINAEMIA TYROSINE KINASE; INOSITOL 1,4,5 TRISPHOSPHATE; PHOSPHOPROTEIN; PLASMA PROTEIN; PLATELET PROTEIN P47;

EID: 0039710379     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.12.3396     Document Type: Article
Times cited : (204)

References (52)
  • 1
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon, D.J. and Anderson, W.F. (1988) A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graphics, 6, 219-220.
    • (1988) J. Mol. Graphics , vol.6 , pp. 219-220
    • Bacon, D.J.1    Anderson, W.F.2
  • 2
    • 0029040199 scopus 로고
    • Protein tyrosine kinases in the initiation of antigen receptor signaling
    • Bolen, J.B. (1995) Protein tyrosine kinases in the initiation of antigen receptor signaling. Curr. Opin. Immunol., 7, 306-311.
    • (1995) Curr. Opin. Immunol. , vol.7 , pp. 306-311
    • Bolen, J.B.1
  • 3
    • 0024825088 scopus 로고
    • High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product
    • Brinkmann, U., Mattes, R.E. and Buckel, P. (1989) High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product. Gene, 85, 109-114.
    • (1989) Gene , vol.85 , pp. 109-114
    • Brinkmann, U.1    Mattes, R.E.2    Buckel, P.3
  • 6
    • 0028033527 scopus 로고
    • B-cell antigen receptor stimulation activates the human Bruton's tyrosine kinase, which is deficient in X-linked agammaglobulinemia
    • de Weers, M., Brouns, G.S., Hinshelwood, S., Kinnon, C., Schuurman, R.K., Hendriks, R.W. and Borst, J. (1994) B-cell antigen receptor stimulation activates the human Bruton's tyrosine kinase, which is deficient in X-linked agammaglobulinemia. J. Biol. Chem., 269, 23857-23860.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23857-23860
    • De Weers, M.1    Brouns, G.S.2    Hinshelwood, S.3    Kinnon, C.4    Schuurman, R.K.5    Hendriks, R.W.6    Borst, J.7
  • 7
    • 0028883178 scopus 로고
    • Phospholipid signaling
    • Divecha, N. and Irvine, R.F. (1995) Phospholipid signaling. Cell, 80, 269-278.
    • (1995) Cell , vol.80 , pp. 269-278
    • Divecha, N.1    Irvine, R.F.2
  • 8
    • 0027945789 scopus 로고
    • Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin
    • Ferguson, K.M., Lemmon, M.A., Schlessinger, J. and Sigler, P. (1994) Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin. Cell, 79, 199-209.
    • (1994) Cell , vol.79 , pp. 199-209
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.4
  • 9
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson, K.M., Lemmon, M.A., Schlessinger, J. and Sigler, P.B. (1995) Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell, 83, 1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 10
    • 0029748612 scopus 로고    scopus 로고
    • Structure-function relationships of the mouse Gap1m. Determination of the inositol 1,3,4,5-tetrakisphosphate-binding domain
    • Fukuda, M. and Mikoshiba, K. (1996) Structure-function relationships of the mouse Gap1m. Determination of the inositol 1,3,4,5-tetrakisphosphate-binding domain. J. Biol. Chem., 271, 18838-18842.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18838-18842
    • Fukuda, M.1    Mikoshiba, K.2
  • 11
    • 0029824848 scopus 로고    scopus 로고
    • Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity
    • Fukuda, M., Kojima, T., Kabayama, H. and Mikoshiba, K. (1996) Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity. J. Biol. Chem., 271, 30303-30306.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30303-30306
    • Fukuda, M.1    Kojima, T.2    Kabayama, H.3    Mikoshiba, K.4
  • 12
    • 0011975439 scopus 로고    scopus 로고
    • PHASES-95: A program package for the processing and analysis of diffraction data from macromolecules
    • in press
    • Furey, W. and Swaminathan, S. (1996) PHASES-95: a program package for the processing and analysis of diffraction data from macromolecules. Methods Enzymol., in press.
    • (1996) Methods Enzymol.
    • Furey, W.1    Swaminathan, S.2
  • 14
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C. and von Hippel, P.H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem., 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 15
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks, S.K., Quinn, A.M. and Hunter, T. (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science, 241, 41-52.
    • (1988) Science , vol.241 , pp. 41-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 16
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan, J.E., Hajduk, P.J., Yoon, H.S. and Fesik, S.W. (1994) Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature, 371, 168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 17
    • 8944250665 scopus 로고    scopus 로고
    • Identification of Bruton's tyrosine kinase (Btk) gene mutations and characterization of the derived proteins in 35 X-linked agammaglobulinemia families: A nationwide study of Btk deficiency in Japan
    • Hashimoto, S. et al. (1996) Identification of Bruton's tyrosine kinase (Btk) gene mutations and characterization of the derived proteins in 35 X-linked agammaglobulinemia families: a nationwide study of Btk deficiency in Japan. Blood, 88, 561-573.
    • (1996) Blood , vol.88 , pp. 561-573
    • Hashimoto, S.1
  • 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
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of proteins
    • Kraulis, P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of proteins. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V. and Wilson, K. (1993) Automated refinement of protein models. Acta Crystallogr., D49, 129-147.
    • (1993) Acta Crystallogr. , vol.D49 , pp. 129-147
    • Lamzin, V.1    Wilson, K.2
  • 23
    • 0028896344 scopus 로고
    • Activation of Tsk and Btk tyrosine kinases by G protein βγ subunits
    • Langhans Rajasekaran, S.A., Wan, Y. and Huang, X.Y. (1995) Activation of Tsk and Btk tyrosine kinases by G protein βγ subunits. Proc. Natl Acad. Sci. USA, 92, 8601-8605.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8601-8605
    • Langhans Rajasekaran, S.A.1    Wan, Y.2    Huang, X.Y.3
  • 26
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • Lemmon, M.A., Ferguson, K.M., O'Brien, R., Sigler, P.B. and Schlessinger, J. (1995) Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc. Natl Acad. Sci. USA, 92, 10472-10476.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    O'Brien, R.3    Sigler, P.B.4    Schlessinger, J.5
  • 27
    • 0028999058 scopus 로고
    • Activation of Bruton's tyrosine kinase (BTK) by a point mutation in its pleckstrin homology (PH) domain
    • Li, T., Tsukada, S., Satterthwaite, A., Havlik, M.H., Park, H., Takatsu, K. and Witte, O.N. (1995) Activation of Bruton's tyrosine kinase (BTK) by a point mutation in its pleckstrin homology (PH) domain. Immunity, 2, 451-460.
    • (1995) Immunity , vol.2 , pp. 451-460
    • Li, T.1    Tsukada, S.2    Satterthwaite, A.3    Havlik, M.H.4    Park, H.5    Takatsu, K.6    Witte, O.N.7
  • 28
    • 0028057108 scopus 로고
    • Raster3D version 2.0 - A program for photorealistic molecular graphics
    • Merrit, E.A. and Murphy, M.E.P. (1994) Raster3D version 2.0 - a program for photorealistic molecular graphics. Acta Crystallogr., D50, 869-873.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 29
    • 0027183541 scopus 로고
    • The PH domain: A common piece in the structural patchwork of signalling proteins
    • Musacchio, A., Gibson, T., Rice, P., Thompson, J. and Saraste, M. (1993) The PH domain: a common piece in the structural patchwork of signalling proteins. Trends Biochem. Sci., 18, 343-348.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 343-348
    • Musacchio, A.1    Gibson, T.2    Rice, P.3    Thompson, J.4    Saraste, M.5
  • 30
    • 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: Struct. Fund. Genet., 11, 281-296.
    • (1991) Proteins: Struct. Fund. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 33
    • 0029983371 scopus 로고    scopus 로고
    • T7 vectors with modified T71ac promoter for expression of proteins in Escherichia coli
    • Peränen, J., Rikkonen, M., Hyvönen, M. and Kääriäinen, L. (1996) T7 vectors with modified T71ac promoter for expression of proteins in Escherichia coli. Anal. Biochem., 236, 371-373.
    • (1996) Anal. Biochem. , vol.236 , pp. 371-373
    • Peränen, J.1    Rikkonen, M.2    Hyvönen, M.3    Kääriäinen, L.4
  • 34
    • 0027305921 scopus 로고
    • Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice
    • Rawlings, D.J. et al. (1993) Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice. Science, 261, 358-361.
    • (1993) Science , vol.261 , pp. 358-361
    • Rawlings, D.J.1
  • 36
    • 0027050183 scopus 로고
    • Phosphoinositide-specific phospholipase C-δ1 binds with high affinity to phospholipid vesicles containing phosphatidylinositol 4,5-bisphosphate
    • Rebecchi, M., Peterson, A. and McLaughlin, S. (1992) Phosphoinositide-specific phospholipase C-δ1 binds with high affinity to phospholipid vesicles containing phosphatidylinositol 4,5-bisphosphate. Biochemistry, 31, 12742-12747.
    • (1992) Biochemistry , vol.31 , pp. 12742-12747
    • Rebecchi, M.1    Peterson, A.2    McLaughlin, S.3
  • 37
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. and Blundell, T. (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.2
  • 38
    • 10544219605 scopus 로고    scopus 로고
    • Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase
    • Salim, K. et al. (1996) Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase. EMBO J., 15, 6241-6250.
    • (1996) EMBO J. , vol.15 , pp. 6241-6250
    • Salim, K.1
  • 39
    • 0028114191 scopus 로고
    • IL-5 receptor-mediated tyrosine phosphorylation of SH2/SH3-containing proteins and activation of Bruton's tyrosine and Janus 2 kinases
    • Sato, S. et al. (1994) IL-5 receptor-mediated tyrosine phosphorylation of SH2/SH3-containing proteins and activation of Bruton's tyrosine and Janus 2 kinases. J. Exp. Med., 180, 2101-2111.
    • (1994) J. Exp. Med. , vol.180 , pp. 2101-2111
    • Sato, S.1
  • 41
    • 0027261447 scopus 로고
    • Colocalization of X-linked agammaglobulinemia and X-linked immunodeficiency genes
    • Thomas, J.D., Sideras, P., Smith, C.I., Vorechovsky, I., Chapman, V. and Paul, W.E. (1993) Colocalization of X-linked agammaglobulinemia and X-linked immunodeficiency genes. Science, 261, 355-358.
    • (1993) Science , vol.261 , pp. 355-358
    • Thomas, J.D.1    Sideras, P.2    Smith, C.I.3    Vorechovsky, I.4    Chapman, V.5    Paul, W.E.6
  • 42
    • 0028246440 scopus 로고
    • Binding of G protein βγ-subunits to pleckstrin homology domains
    • Touhara, K., Inglese, J., Pitcher, J.A., Shaw, G. and Lefkowitz, R.J. (1994) Binding of G protein βγ-subunits to pleckstrin homology domains. J. Biol. Chem., 269, 10217-10220.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10217-10220
    • Touhara, K.1    Inglese, J.2    Pitcher, J.A.3    Shaw, G.4    Lefkowitz, R.J.5
  • 43
    • 84913050729 scopus 로고
    • An efficient general-purpose least-square refinement program for macromolecular structures
    • Tronrud, D.E., Ten Eyck, L.F. and Matthews, B.W. (1987) An efficient general-purpose least-square refinement program for macromolecular structures. Acta Crystallogr., A43, 489-501.
    • (1987) Acta Crystallogr. , vol.A43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 44
    • 0027399081 scopus 로고
    • Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia
    • Tsukada, S. et al. (1993) Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia. Cell, 72, 279-290.
    • (1993) Cell , vol.72 , pp. 279-290
    • Tsukada, S.1
  • 45
    • 0028173394 scopus 로고
    • Binding of βγ subunits of trimeric G proteins to the PH domain of Bruton tyrosine kinase
    • Tsukada, S., Simon, M.I., Witte, O. and Katz, A. (1994) Binding of βγ subunits of trimeric G proteins to the PH domain of Bruton tyrosine kinase. Proc. Natl Acad. Sci. USA, 91, 11256-11260.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11256-11260
    • Tsukada, S.1    Simon, M.I.2    Witte, O.3    Katz, A.4
  • 46
    • 0027441332 scopus 로고
    • The gene involved in X-linked agammaglobulinemia is a member of the src family of protein-tyrosine kinases
    • Vetrie, D. et al. (1993) The gene involved in X-linked agammaglobulinemia is a member of the src family of protein-tyrosine kinases. Nature, 361, 226-233.
    • (1993) Nature , vol.361 , pp. 226-233
    • Vetrie, D.1
  • 47
    • 0027941128 scopus 로고
    • Tec homology (TH) adjacent to the PH domain
    • Vihinen, M., Nilsson, L. and Smith, C.I. (1994) Tec homology (TH) adjacent to the PH domain. FEBS Lett., 350, 263-265.
    • (1994) FEBS Lett. , vol.350 , pp. 263-265
    • Vihinen, M.1    Nilsson, L.2    Smith, C.I.3
  • 50
    • 0025398721 scopus 로고
    • WHAT if - A molecular modelling and drug design program
    • Vriend, G. (1990) WHAT IF - a molecular modelling and drug design program. J. Mol. Graphics, 8, 52-56.
    • (1990) J. Mol. Graphics , vol.8 , pp. 52-56
    • Vriend, G.1
  • 51
    • 0028564915 scopus 로고
    • The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C
    • Yao, L., Kawakami, Y. and Kawakami, T. (1994) The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C. Proc. Natl Acad. Sci. USA, 91, 9175-9179.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9175-9179
    • Yao, L.1    Kawakami, Y.2    Kawakami, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.