메뉴 건너뛰기




Volumn 276, Issue 2, 1998, Pages 461-478

Solution structure of the C-terminal SH2 domain of the p85α regulatory subunit of phosphoinositide 3-kinase

Author keywords

Phosphoinositide 3 kinase; Phosphotyrosine; Platelet derived growth factor receptor; SH2 domain; Solution structure

Indexed keywords

MUTANT PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOTYROSINE; PLATELET DERIVED GROWTH FACTOR RECEPTOR;

EID: 0032548993     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1562     Document Type: Article
Times cited : (48)

References (60)
  • 1
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed-field gradient NMR self-diffusion measurements
    • Altieri A.S., Hinton D.P., Byrd R.A. Association of biomolecular systems via pulsed-field gradient NMR self-diffusion measurements. J. Am. Chem. Soc. 117:1995;7566-7567
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Hinton, D.P.2    Byrd, R.A.3
  • 2
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C., Xia T., Billeter M., Güntert P., Wüthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR. 6:1995;1-10
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 3
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax A., Grzesiek S. Methodological advances in protein NMR. Acct. Chem. Res. 26:1993;131-138
    • (1993) Acct. Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 4
    • 0024311951 scopus 로고
    • Comparison of the high-resolution structures of the α-amylase inhibitor Tendamistat determined by nuclear magnetic resonance in solution and X-ray diffraction in single crystals
    • Billeter M., Kline A., Braun W., Huber R., Wüthrich K. Comparison of the high-resolution structures of the α-amylase inhibitor Tendamistat determined by nuclear magnetic resonance in solution and X-ray diffraction in single crystals. J. Mol. Biol. 206:1989;677-687
    • (1989) J. Mol. Biol. , vol.206 , pp. 677-687
    • Billeter, M.1    Kline, A.2    Braun, W.3    Huber, R.4    Wüthrich, K.5
  • 6
    • 0029894672 scopus 로고    scopus 로고
    • Structure of a specific peptide complex of the carboxy-terminal SH2 domain from the p85α subunit of phosphatidylinositol 3-kinase
    • Breeze A.L., Kara B.V., Barratt D.G., Anderson M., Smith J.C., Luke R.W., Best J.R., Cartlidge S.A. Structure of a specific peptide complex of the carboxy-terminal SH2 domain from the p85α subunit of phosphatidylinositol 3-kinase. EMBO J. 15:1996;3579-3589
    • (1996) EMBO J. , vol.15 , pp. 3579-3589
    • Breeze, A.L.1    Kara, B.V.2    Barratt, D.G.3    Anderson, M.4    Smith, J.C.5    Luke, R.W.6    Best, J.R.7    Cartlidge, S.A.8
  • 9
    • 33748476849 scopus 로고
    • Suppression of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence
    • Cavanagh J., Rance M. Suppression of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence. J. Magn. Reson. 96:1992;670-678
    • (1992) J. Magn. Reson. , vol.96 , pp. 670-678
    • Cavanagh, J.1    Rance, M.2
  • 10
    • 0024351231 scopus 로고
    • Determination of the three dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy
    • Clore G.M., Gronenborn A.M. Determination of the three dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy. CRC Crit. Rev. Biochem. Mol. Biol. 24:1989;479-564
    • (1989) CRC Crit. Rev. Biochem. Mol. Biol. , vol.24 , pp. 479-564
    • Clore, G.M.1    Gronenborn, A.M.2
  • 12
    • 0029400890 scopus 로고
    • Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: Application to myosin light chain 2
    • Dingley A.J., Mackay J.P., Chapman B.E., Morris M.B., Kuchel P.W., Hambly B.D., King G.F. Measuring protein self-association using pulsed-field-gradient NMR spectroscopy application to myosin light chain 2. J. Biomol. NMR. 6:1995;321-328
    • (1995) J. Biomol. NMR , vol.6 , pp. 321-328
    • Dingley, A.J.1    MacKay, J.P.2    Chapman, B.E.3    Morris, M.B.4    Kuchel, P.W.5    Hambly, B.D.6    King, G.F.7
  • 13
    • 0027502504 scopus 로고
    • Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck
    • Eck M.J., Shoelson S.E., Harrison S.C. 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.J.1    Shoelson, S.E.2    Harrison, S.C.3
  • 14
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Güntert P., Braun W., Wüthrich K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217:1991;517-530
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 15
    • 0000088628 scopus 로고
    • Processing of multi-dimensional NMR data with the new software PROSA
    • Güntert P., Dötsch V., Wider G., Wüthrich K. Processing of multi-dimensional NMR data with the new software PROSA. J. Biomol. NMR. 2:1992;619-629
    • (1992) J. Biomol. NMR , vol.2 , pp. 619-629
    • Güntert, P.1    Dötsch, V.2    Wider, G.3    Wüthrich, K.4
  • 17
    • 0028243961 scopus 로고
    • Phosphopeptide binding to the N-terminal SH2 domain of the p85α subunit of PI 3′-kinase: A heteronuclear NMR study
    • Hensmann M., Booker G.W., Panayotou G., Boyd J., Linacre J., Waterfield M., Campbell I.D. Phosphopeptide binding to the N-terminal SH2 domain of the p85α subunit of PI 3′-kinase a heteronuclear NMR study. Protein Sci. 3:1994;1020-1030
    • (1994) Protein Sci. , vol.3 , pp. 1020-1030
    • Hensmann, M.1    Booker, G.W.2    Panayotou, G.3    Boyd, J.4    Linacre, J.5    Waterfield, M.6    Campbell, I.D.7
  • 18
    • 0028120902 scopus 로고
    • Phosphatidylinositol 3-kinase activation is mediated by high-affinity interactions between distinct domains within the p110 and p85 subunits
    • Holt K.H,., Olson A.L., Moye-Rowley S., Pessin J.E. Phosphatidylinositol 3-kinase activation is mediated by high-affinity interactions between distinct domains within the p110 and p85 subunits. Mol. Cell. Biol. 14:1994;42-49
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 42-49
    • Holt, K.H.1    Olson, A.L.2    Moye-Rowley, S.3    Pessin, J.E.4
  • 19
    • 0028486018 scopus 로고
    • Phosphatidylinositol 3-kinase
    • Kapeller R., Cantley L.C. Phosphatidylinositol 3-kinase. Bioessays. 16:1994;565-576
    • (1994) Bioessays , vol.16 , pp. 565-576
    • Kapeller, R.1    Cantley, L.C.2
  • 20
    • 0026557517 scopus 로고
    • Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo
    • Kashishian A., Kazlauskas A., Cooper J.A. Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo. EMBO J. 11:1992;1373-1382
    • (1992) EMBO J. , vol.11 , pp. 1373-1382
    • Kashishian, A.1    Kazlauskas, A.2    Cooper, J.A.3
  • 25
    • 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
  • 26
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A., Ernst R.R., Wüthrich K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95:1980;1-6
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 28
    • 0030000912 scopus 로고    scopus 로고
    • Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases
    • Kuszewski J., Gronenborn A.M., Clore G.M. Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases. Protein Sci. 5:1996;1067-1080
    • (1996) Protein Sci. , vol.5 , pp. 1067-1080
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 30
    • 0028773467 scopus 로고
    • Crystal-structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase
    • Lee C.H., Kominos D., Jacques S., Margolis B., Schlessinger J., Shoelson S.E., Kuriyan J. Crystal-structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase. Structure. 2:1994;423-438
    • (1994) Structure , vol.2 , pp. 423-438
    • Lee, C.H.1    Kominos, D.2    Jacques, S.3    Margolis, B.4    Schlessinger, J.5    Shoelson, S.E.6    Kuriyan, J.7
  • 32
    • 0029693096 scopus 로고    scopus 로고
    • Separation of intramolecular NOE and exchange peaks in water exchange spectroscopy using spin-echo filters
    • Mori S., Berg J., van Zijl P.C.M. Separation of intramolecular NOE and exchange peaks in water exchange spectroscopy using spin-echo filters. J. Biomol. NMR. 7:1996;77-82
    • (1996) J. Biomol. NMR , vol.7 , pp. 77-82
    • Mori, S.1    Berg, J.2    Van Zijl, P.C.M.3
  • 33
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance 3-dimensional NMR experiments with improved sensitivity
    • Muhandiram D.R., Kay L.E. Gradient-enhanced triple-resonance 3-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. (B). 103:1994;203-216
    • (1994) J. Magn. Reson. (B) , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 35
    • 0024323295 scopus 로고
    • A general method of site-specific mutagenesis using a modification of the Taq polymerase chain reaction
    • Nelson R., Long G.L. A general method of site-specific mutagenesis using a modification of the Taq polymerase chain reaction. Anal. Biochem. 180:1989;147-151
    • (1989) Anal. Biochem. , vol.180 , pp. 147-151
    • Nelson, R.1    Long, G.L.2
  • 37
    • 0029878266 scopus 로고    scopus 로고
    • Crystal-structure of the PI-3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes
    • Nolte R.T., Eck M.J., Schlessinger J., Shoelson S.E., Harrison S.C. Crystal-structure of the PI-3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes. Nature Struct. Biol. 3:1996;364-374
    • (1996) Nature Struct. Biol. , vol.3 , pp. 364-374
    • Nolte, R.T.1    Eck, M.J.2    Schlessinger, J.3    Shoelson, S.E.4    Harrison, S.C.5
  • 38
    • 0029283884 scopus 로고
    • Chemical shifts and three-dimensional protein structures
    • Oldfield E. Chemical shifts and three-dimensional protein structures. J. Biomol. NMR. 5:1995;217-225
    • (1995) J. Biomol. NMR , vol.5 , pp. 217-225
    • Oldfield, E.1
  • 40
    • 0026669472 scopus 로고
    • 3-Dimensional solution structure of the Src homology-2 domain of c-Abl
    • Overduin M., Rios C.B., Mayer B.J., Baltimore D., Cowburn D. 3-Dimensional solution structure of the Src homology-2 domain of c-Abl. Cell. 70:1992;697-704
    • (1992) Cell , vol.70 , pp. 697-704
    • Overduin, M.1    Rios, C.B.2    Mayer, B.J.3    Baltimore, D.4    Cowburn, D.5
  • 41
    • 0027195236 scopus 로고
    • Interactions between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor β-receptor sequences: Analysis of kinetic parameters by a novel biosensor-based approach
    • Panayotou G., Gish G., Truong O., Gout I., Dhand R., Fry M.J., Hiles I., Pawson T., Waterfield M.D. Interactions between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor β-receptor sequences analysis of kinetic parameters by a novel biosensor-based approach. Mol. Cell. Biol. 13:1993;3567-3576
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3567-3576
    • Panayotou, G.1    Gish, G.2    Truong, O.3    Gout, I.4    Dhand, R.5    Fry, M.J.6    Hiles, I.7    Pawson, T.8    Waterfield, M.D.9
  • 42
    • 0028354446 scopus 로고
    • Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-γ1 complexed with a high affinity binding peptide
    • Pascal S.M., Singer A.U., Gish G., Yamazaki T., Shoelson S.E., Pawson T., Kay L.E., Forman-Kay J.D. Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-γ1 complexed with a high affinity binding peptide. Cell. 77:1994;461-472
    • (1994) Cell , vol.77 , pp. 461-472
    • Pascal, S.M.1    Singer, A.U.2    Gish, G.3    Yamazaki, T.4    Shoelson, S.E.5    Pawson, T.6    Kay, L.E.7    Forman-Kay, J.D.8
  • 44
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini U., Sørensen O.W., Ernst R.R. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 104:1982;6800
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6800
    • Piantini, U.1    Sørensen, O.W.2    Ernst, R.R.3
  • 47
    • 0028909206 scopus 로고
    • Regulation of phosphatidylinositol 3′-kinase by tyrosyl phosphoproteins: Full activation requires occupancy of both SH2 domains in the 85-kDa regulatory subunit
    • Rordorf-Nikolic T., Van Horn D.J., Chen D., White M.F., Backer J.M. Regulation of phosphatidylinositol 3′-kinase by tyrosyl phosphoproteins full activation requires occupancy of both SH2 domains in the 85-kDa regulatory subunit. J. Biol. Chem. 270:1995;3662-3666
    • (1995) J. Biol. Chem. , vol.270 , pp. 3662-3666
    • Rordorf-Nikolic, T.1    Van Horn, D.J.2    Chen, D.3    White, M.F.4    Backer, J.M.5
  • 48
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker S.B., Hajduk P.J., Meadows R.P., Fesik S.W. Discovering high-affinity ligands for proteins SAR by NMR. Science. 274:1996;1531-1534
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 50
    • 0028863102 scopus 로고
    • A single-point mutation switches the specificity of group-III Src homology SH2 domains to that of group-I SH2 domains
    • Songyang Z., Gish G., Mbamalu G., Pawson T., Cantley L.C. A single-point mutation switches the specificity of group-III Src homology SH2 domains to that of group-I SH2 domains. J. Biol. Chem. 270:1995;26029-26032
    • (1995) J. Biol. Chem. , vol.270 , pp. 26029-26032
    • Songyang, Z.1    Gish, G.2    Mbamalu, G.3    Pawson, T.4    Cantley, L.C.5
  • 51
    • 0347610773 scopus 로고
    • 13C nuclear magnetic resonance chemical shifts
    • 13C nuclear magnetic resonance chemical shifts. J. Amer. Chem. Soc. 113:1991;5490-5492
    • (1991) J. Amer. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 52
    • 44049114111 scopus 로고
    • Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets
    • Szyperski T., Güntert P., Otting G., Wüthrich K. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets. J. Magn. Reson. 99:1992;552-560
    • (1992) J. Magn. Reson. , vol.99 , pp. 552-560
    • Szyperski, T.1    Güntert, P.2    Otting, G.3    Wüthrich, K.4
  • 53
    • 0030992837 scopus 로고    scopus 로고
    • Signalling through the lipid products of phosphoinositide-3-OH kinase
    • Toker A., Cantley L.C. Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature. 387:1997;673-676
    • (1997) Nature , vol.387 , pp. 673-676
    • Toker, A.1    Cantley, L.C.2
  • 56
    • 0026698924 scopus 로고
    • Crystal-structure of the phosphotyrosine recognition domain SH2 of v-Src complexed with tyrosine-phosphorylated peptides
    • Waksman G., Kominos D., Robertson S.C., Pant N., Baltimore D., Birge R.B., Kuriyan J. Crystal-structure of the phosphotyrosine recognition domain SH2 of v-Src complexed with tyrosine-phosphorylated peptides. Nature. 358:1992;646-653
    • (1992) Nature , vol.358 , pp. 646-653
    • Waksman, G.1    Kominos, D.2    Robertson, S.C.3    Pant, N.4    Baltimore, D.5    Birge, R.B.6    Kuriyan, J.7
  • 57
    • 0027409064 scopus 로고
    • Binding of a high-affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal-structures of the complexed and peptide-free forms
    • Waksman G., Shoelson S.E., Pant N., Cowburn D., Kuriyan J. Binding of a high-affinity phosphotyrosyl peptide to the Src SH2 domain crystal-structures of the complexed and peptide-free forms. Cell. 72:1993;779-790
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 59
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of Drk in folded and unfolded states using enhanced-sensitivity pulsed-field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of Drk in folded and unfolded states using enhanced-sensitivity pulsed-field gradient NMR techniques. J. Biomol. NMR. 4:1994;845-858
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.W.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.