메뉴 건너뛰기




Volumn 6, Issue 9, 1997, Pages 1910-1919

pH titration studies of an SH2 domain-phosphopeptide complex: Unusual histidine and phosphate pK(a) values

Author keywords

Histidine; NMR; Phospholipase C ; Phosphotyrosine; pK(a) determination; SH2 domain

Indexed keywords

PHOSPHOTYROSINE; PLATELET DERIVED GROWTH FACTOR RECEPTOR;

EID: 0030767535     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060912     Document Type: Article
Times cited : (41)

References (54)
  • 3
    • 0022925238 scopus 로고
    • 15N NMR spectroscopy of hydrogen-bonding interactions in the active site of serine proteases: Evidence for a moving histidine mechanism
    • 15N NMR spectroscopy of hydrogen-bonding interactions in the active site of serine proteases: Evidence for a moving histidine mechanism. Biochemistry 25:7751-7759.
    • (1986) Biochemistry , vol.25 , pp. 7751-7759
    • Bachovchin, W.W.1
  • 8
    • 0027502504 scopus 로고
    • Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p561ck
    • Eck MJ, Shoelson SE, Harrison SC. 1993. Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p561ck. Nature 362:81-91.
    • (1993) Nature , vol.362 , pp. 81-91
    • Eck, M.J.1    Shoelson, S.E.2    Harrison, S.C.3
  • 10
  • 11
    • 0000041361 scopus 로고
    • A common sense approach to peak picking in two-, three- And four-dimensional spectra using automatic computer analysis of contour diagrams
    • Garrett DS, Powers R, Gronenborn AM, Clore GM. 1991. A common sense approach to peak picking in two-, three-and four-dimensional spectra using automatic computer analysis of contour diagrams. J Magn Reson 95:214-220.
    • (1991) J Magn Reson , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 13
    • 0029066848 scopus 로고
    • Theory of electrostatic interactions in macromolecules
    • Gilson MK. 1995. Theory of electrostatic interactions in macromolecules. Curr Opin Struct Biol 5:216-223.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 216-223
    • Gilson, M.K.1
  • 16
    • 0030042698 scopus 로고    scopus 로고
    • Correlation between dynamics and high affinity binding in an SH2 domain interaction
    • Kay LE, Muhandiram DR, Farrow NA, Aubin Y, Forman-Kay JD. 1996. Correlation between dynamics and high affinity binding in an SH2 domain interaction. Biochemistry 35:361-368.
    • (1996) Biochemistry , vol.35 , pp. 361-368
    • Kay, L.E.1    Muhandiram, D.R.2    Farrow, N.A.3    Aubin, Y.4    Forman-Kay, J.D.5
  • 17
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 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
  • 18
    • 0027264591 scopus 로고
    • Identification of residues in the β platelet-derived growth factor receptor that confer specificity for binding to phospholipase C-γ1
    • Larose L, Gish G, Shoelson S, Pawson T. 1993. Identification of residues in the β platelet-derived growth factor receptor that confer specificity for binding to phospholipase C-γ1. Oncogene 8:2493-2499.
    • (1993) Oncogene , vol.8 , pp. 2493-2499
    • Larose, L.1    Gish, G.2    Shoelson, S.3    Pawson, T.4
  • 21
    • 0025871717 scopus 로고
    • Neutral imidazole is the electrophile in the reaction catalyzed by triosphosphate isomerase: Structural origins and catalytic implications
    • Lodi PJ, Knowles JR. 1991. Neutral imidazole is the electrophile in the reaction catalyzed by triosphosphate isomerase: Structural origins and catalytic implications. Biochemistry 30:6948-6956.
    • (1991) Biochemistry , vol.30 , pp. 6948-6956
    • Lodi, P.J.1    Knowles, J.R.2
  • 22
    • 0027190867 scopus 로고
    • Direct evidence for the exploitation of an α-helix in the catalytic mechanism of triosephosphate isomerase
    • Lodi PJ, Knowles JR. 1993. Direct evidence for the exploitation of an α-helix in the catalytic mechanism of triosephosphate isomerase. Biochemistry 32:4338-4343.
    • (1993) Biochemistry , vol.32 , pp. 4338-4343
    • Lodi, P.J.1    Knowles, J.R.2
  • 23
    • 0028082018 scopus 로고
    • Comparison of calcium-dependent conformational changes in the N-terminal SH2 domains of p85 and GAP defines distinct properties for SH2 domains
    • Mahadevan D, Thanki N, McPhie P, Beeler JF, Yu J-C, Wlodawer A, Heidaran MA. 1994. Comparison of calcium-dependent conformational changes in the N-terminal SH2 domains of p85 and GAP defines distinct properties for SH2 domains. Biochemistry 33:746-754.
    • (1994) Biochemistry , vol.33 , pp. 746-754
    • Mahadevan, D.1    Thanki, N.2    McPhie, P.3    Beeler, J.F.4    Yu, J.-C.5    Wlodawer, A.6    Heidaran, M.A.7
  • 25
    • 0026453585 scopus 로고
    • Identification of residues in GTPase-activating protein Src Homology 2 domains that control binding to tyrosine phosphorylated growth factor receptors and p62
    • Marangere LEM, Pawson T. 1992. Identification of residues in GTPase-activating protein Src Homology 2 domains that control binding to tyrosine phosphorylated growth factor receptors and p62. J Biol Chem 267:22779-22786.
    • (1992) J Biol Chem , vol.267 , pp. 22779-22786
    • Marangere, L.E.M.1    Pawson, T.2
  • 26
    • 1842339755 scopus 로고
    • Waltham, Massachusetts
    • Molecular Simulations Inc. 1993. QUANTA, version 4.0. Waltham, Massachusetts.
    • (1993) QUANTA, Version 4.0
  • 28
    • 0027521783 scopus 로고
    • Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor
    • Nishimura R, Li W, Kashishian A, Mondino A, Zhou M, Cooper J, Schlessinger J. 1993. Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor. Mol Cell Biol 75:6889-6896.
    • (1993) Mol Cell Biol , vol.75 , pp. 6889-6896
    • Nishimura, R.1    Li, W.2    Kashishian, A.3    Mondino, A.4    Zhou, M.5    Cooper, J.6    Schlessinger, J.7
  • 29
    • 0029878266 scopus 로고    scopus 로고
    • Crystal structure of the PI3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes
    • Nolte R, Eck MJ, Schlessinger J, Shoelson SE, Harrison SC. 1996. Crystal structure of the PI3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes. Nat Struct Biol 3:364-374.
    • (1996) Nat Struct Biol , vol.3 , pp. 364-374
    • Nolte, R.1    Eck, M.J.2    Schlessinger, J.3    Shoelson, S.E.4    Harrison, S.C.5
  • 30
    • 0001461682 scopus 로고
    • Examination of titration behavior
    • Nozaki Y, Tanford C. 1967. Examination of titration behavior. Methods Enzvmol 11:715-734.
    • (1967) Methods Enzvmol , vol.11 , pp. 715-734
    • Nozaki, Y.1    Tanford, C.2
  • 31
    • 0027468233 scopus 로고
    • A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of ras guanine nucleotide exchange, Sos
    • Olivier JP, Raabe T, Henkemeyer M, Dickson B, Mbamalu G, Margolis B, Schlessinger J, Hafen E, Pawson T. 1993. A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of ras guanine nucleotide exchange, Sos. Cell 75:179-191.
    • (1993) Cell , vol.75 , pp. 179-191
    • Olivier, J.P.1    Raabe, T.2    Henkemeyer, M.3    Dickson, B.4    Mbamalu, G.5    Margolis, B.6    Schlessinger, J.7    Hafen, E.8    Pawson, T.9
  • 32
    • 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, End P, Truong O, Gout I, Dhand R, Fry MJ, Hiles I, Pawson T, Waterfield MD. 1993. 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 13:3567-3576.
    • (1993) Mol Cell Biol , vol.13 , pp. 3567-3576
    • Panayotou, G.1    Gish, G.2    End, P.3    Truong, O.4    Gout, I.5    Dhand, R.6    Fry, M.J.7    Hiles, I.8    Pawson, T.9    Waterfield, M.D.10
  • 33
    • 0028354446 scopus 로고
    • Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-γ1 complexed with a high affinity binding peptide
    • Pascal SM, Singer AU, Gish G, Yamazaki T, Shoelson SE, Pawson T, Kay LE, Forman-Kay JD. 1994. Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-γ1 complexed with a high affinity binding peptide. Cell 77:461-472.
    • (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
  • 35
    • 0029142571 scopus 로고
    • Structural and dynamical characterization of the phosphotyrosine binding region of a Src Homology 2 domain-phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches
    • Pascal SM, Yamazaki T, Singer AU, Kay LE, Forman-Kay J. 1995. Structural and dynamical characterization of the phosphotyrosine binding region of a Src Homology 2 domain-phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches. Biochemistry 54:11353-11362.
    • (1995) Biochemistry , vol.54 , pp. 11353-11362
    • Pascal, S.M.1    Yamazaki, T.2    Singer, A.U.3    Kay, L.E.4    Forman-Kay, J.5
  • 36
    • 0027456412 scopus 로고
    • Glc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques
    • Glc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques. Protein Sci 2:543-558.
    • (1993) Protein Sci , vol.2 , pp. 543-558
    • Pelton, J.G.1    Torchia, D.A.2    Meadow, N.D.3    Roseman, S.4
  • 37
    • 0029562951 scopus 로고
    • 1 in solution: Correlation with NMR and x-ray data and insights into biological function
    • 1 in solution: Correlation with NMR and x-ray data and insights into biological function. J Mol Biol 254:771-792.
    • (1995) J Mol Biol , vol.254 , pp. 771-792
    • Philippopoulos, M.1    Lim, C.2
  • 38
    • 0030023620 scopus 로고    scopus 로고
    • Ionization equilibria for side-chain carboxyl groups in oxidized and reduced human thioredoxin and in the complex with its target peptide from the transcription factor NFκB
    • Qin J, Clore GM, Gronenbom A. 1996. Ionization equilibria for side-chain carboxyl groups in oxidized and reduced human thioredoxin and in the complex with its target peptide from the transcription factor NFκB. Biochemistry 35:7-13.
    • (1996) Biochemistry , vol.35 , pp. 7-13
    • Qin, J.1    Clore, G.M.2    Gronenbom, A.3
  • 39
    • 0029081101 scopus 로고
    • SH2 domain structure and function
    • Schaffhausen B. 1995. SH2 domain structure and function. Biochim Biophys Acta 1242:61-75.
    • (1995) Biochim Biophys Acta , vol.1242 , pp. 61-75
    • Schaffhausen, B.1
  • 43
    • 0021103512 scopus 로고
    • 1H-NMR Study on the tautomerism of the imidazole ring of histitine residues. 1. Microscopic pK values and molar ratios of tautomers in histidine-containing peptides
    • 1H-NMR Study on the tautomerism of the imidazole ring of histitine residues. 1. Microscopic pK values and molar ratios of tautomers in histidine-containing peptides. Biochim Biophys Acta 742:576-585.
    • (1983) Biochim Biophys Acta , vol.742 , pp. 576-585
    • Tanokura, M.1
  • 44
    • 0029670932 scopus 로고    scopus 로고
    • 1H NMR spectroscopy of the catalytic histidine in choromethyl ketone-inhibited complexes of serine proteases
    • 1H NMR spectroscopy of the catalytic histidine in choromethyl ketone-inhibited complexes of serine proteases. Biochemistry 55:2437-2444.
    • (1996) Biochemistry , vol.55 , pp. 2437-2444
    • Tsilikonas, E.1    Rao, T.2    Gutheil, W.G.3    Bachovchin, W.W.4
  • 47
    • 0024830776 scopus 로고
    • Phosphorus-31 NMR of phosphoproteins
    • Vogel HJ. 1989. Phosphorus-31 NMR of phosphoproteins. Methods Enzymol 177:263-282.
    • (1989) Methods Enzymol , vol.177 , pp. 263-282
    • Vogel, H.J.1
  • 48
    • 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 SE, Pant N, Cowhum D, Kuriyan J. 1993. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 Domain: Crystal structures of the complexed and peptide-free forms. Cell 72:779-790.
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowhum, D.4    Kuriyan, J.5
  • 54
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in the folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in the folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR 4:845-858.
    • (1994) J Biomol NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.