메뉴 건너뛰기




Volumn 43, Issue 46, 2004, Pages 14555-14565

Epitope mapping of the phosphorylation motif of the HIV-1 protein Vpu bound to the selective monoclonal antibody using TRNOESY and STD NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIBODIES; ANTIGENS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POLYPEPTIDES; SIGNALING; VIRUSES;

EID: 8744303694     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0492861     Document Type: Article
Times cited : (11)

References (51)
  • 2
    • 0024381228 scopus 로고
    • Molecular and biochemical analyses of human immunodeficiency virus type 1 vpu protein
    • Strebel, K., Klimkait, T., Maldarelli, F., and Martin, M. A. (1989) Molecular and biochemical analyses of human immunodeficiency virus type 1 vpu protein, J. Virol. 63, 3784-3791.
    • (1989) J. Virol. , vol.63 , pp. 3784-3791
    • Strebel, K.1    Klimkait, T.2    Maldarelli, F.3    Martin, M.A.4
  • 3
    • 0023677668 scopus 로고
    • A novel gene of HIV-1, Vpu, and its 16 kilodalton product
    • Strebel, K., Klimkait, T., and Martin, M. A. (1988) A novel gene of HIV-1, Vpu, and its 16 kilodalton product, Science 241, 1221-1223.
    • (1988) Science , vol.241 , pp. 1221-1223
    • Strebel, K.1    Klimkait, T.2    Martin, M.A.3
  • 4
    • 0026452726 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4
    • Willey, R. L., Maldarelli, F., Martin, M. A., and Strebel, K. (1992) Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4, J. Virol. 66, 7193-7200.
    • (1992) J. Virol. , vol.66 , pp. 7193-7200
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 5
    • 0032012456 scopus 로고    scopus 로고
    • A novel human WD protein, h-βTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
    • Margottin, F., Bour, S., Durand, H., Selig, L., Benichou, S., Richard, V., Thomas, D., Strebel, K., and Benarous, R. (1998) A novel human WD protein, h-βTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif, Mol. Cell 1, 565-574.
    • (1998) Mol. Cell , vol.1 , pp. 565-574
    • Margottin, F.1    Bour, S.2    Durand, H.3    Selig, L.4    Benichou, S.5    Richard, V.6    Thomas, D.7    Strebel, K.8    Benarous, R.9
  • 6
    • 0028349047 scopus 로고
    • Differential activities of the human immunodeficiency virus type I-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments
    • Schubert, U., and Strebel, K. (1994) Differential activities of the human immunodeficiency virus type I-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments, J. Virol. 68, 2260-2271.
    • (1994) J. Virol. , vol.68 , pp. 2260-2271
    • Schubert, U.1    Strebel, K.2
  • 8
    • 0033068154 scopus 로고    scopus 로고
    • The SCF β-TrCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro
    • Winston, J. T., Strack, P., Beer-Romero, P., Chu, C. Y., Elledge, S. J., and Harper, J. W. (1999) The SCF β-TrCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro, Genes Dev. 13, 270-283.
    • (1999) Genes Dev. , vol.13 , pp. 270-283
    • Winston, J.T.1    Strack, P.2    Beer-Romero, P.3    Chu, C.Y.4    Elledge, S.J.5    Harper, J.W.6
  • 13
    • 0024496497 scopus 로고
    • A monoclonal antibody against the platelet fibronogen receptor contains a sequence that mimics a receptor recognition domain in fibrinogen
    • Taub, R., Gould, R. J., Garsky, V. M., Ciccarone, T. M., Hoxie, J., Friedman, P. A., and Shattil, S. J. (1989) A monoclonal antibody against the platelet fibronogen receptor contains a sequence that mimics a receptor recognition domain in fibrinogen, J. Biol. Chem. 264, 259-265.
    • (1989) J. Biol. Chem. , vol.264 , pp. 259-265
    • Taub, R.1    Gould, R.J.2    Garsky, V.M.3    Ciccarone, T.M.4    Hoxie, J.5    Friedman, P.A.6    Shattil, S.J.7
  • 14
    • 0026808747 scopus 로고
    • Functional validation of ligand mimicry by anti-receptor antibodies: Structural and therapeutic implications
    • Taub, R., and Greene, M. I. (1992) Functional validation of ligand mimicry by anti-receptor antibodies: structural and therapeutic implications, Biochemistry 31, 7431-7435.
    • (1992) Biochemistry , vol.31 , pp. 7431-7435
    • Taub, R.1    Greene, M.I.2
  • 15
    • 0026625737 scopus 로고
    • Localization of the cross-linking sites of RGD and KQAGDV peptides to the isolated fibrinogen receptor, the human platelet integrin glycoprotein IIb/IIIa. Influence of peptide length
    • Calvete, J. J., Schafer, W., Mann, K., Henschen, A., and Gonzalez-Rodriguez, J. (1992) Localization of the cross-linking sites of RGD and KQAGDV peptides to the isolated fibrinogen receptor, the human platelet integrin glycoprotein IIb/IIIa. Influence of peptide length, Eur. J. Biochem. 206, 759-765.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 759-765
    • Calvete, J.J.1    Schafer, W.2    Mann, K.3    Henschen, A.4    Gonzalez-Rodriguez, J.5
  • 17
    • 0028728698 scopus 로고
    • Recent Developments in Transferred NOE Methods
    • Ni, F. (1994) Recent Developments in Transferred NOE Methods, Prog. Nucl. Magn. Reson. Spectrosc. 26, 517-606.
    • (1994) Prog. Nucl. Magn. Reson. Spectrosc. , vol.26 , pp. 517-606
    • Ni, F.1
  • 18
    • 0033538283 scopus 로고    scopus 로고
    • Detecting binding affinity to immobilized receptor proteins in compound libraries by HR-MAS STD NMR
    • Klein, J., Meinecke, R., Mayer, M., and Meyer, B. (1999) Detecting binding affinity to immobilized receptor proteins in compound libraries by HR-MAS STD NMR, J. Am. Chem. Soc. 121, 5336-5337.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5336-5337
    • Klein, J.1    Meinecke, R.2    Mayer, M.3    Meyer, B.4
  • 19
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • Mayer, M., and Meyer, B. (1999) Characterization of ligand binding by saturation transfer difference NMR spectroscopy, Angew. Chem., Int. Ed. Engl. 38, 1784-1788.
    • (1999) Angew. Chem., Int. Ed. Engl. , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 20
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • Mayer, M., and Meyer, B. (2001) Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor, J. Am. Chem. Soc. 123, 6108-6117.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 21
    • 0027361390 scopus 로고
    • Experimental NMR techniques for studies of protein-ligand interactions
    • Otting, G. (1993) Experimental NMR techniques for studies of protein-ligand interactions, Curr. Open. Struct. Biol. 3, 760-768.
    • (1993) Curr. Open. Struct. Biol. , vol.3 , pp. 760-768
    • Otting, G.1
  • 22
    • 0037006971 scopus 로고    scopus 로고
    • Antibiotic Resistance Peptides; Interaction of Peptides Conferring Macrolides and Ketolide Resistance with Staphylococcus aureus Ribosomes. Conformation of Bound Peptides As Determined by Transferred NOE Experiments
    • Verdier, L., Gharbi-Benarous, J., Bertho, G., Mauvais, P., and Girault, J. P. (2002) Antibiotic Resistance Peptides; Interaction of Peptides Conferring Macrolides and Ketolide Resistance with Staphylococcus aureus Ribosomes. Conformation of Bound Peptides As Determined by Transferred NOE Experiments, Biochemistry 41, 4218-4229.
    • (2002) Biochemistry , vol.41 , pp. 4218-4229
    • Verdier, L.1    Gharbi-Benarous, J.2    Bertho, G.3    Mauvais, P.4    Girault, J.P.5
  • 24
    • 0002769836 scopus 로고
    • Etude par RMN-2D des interactions antigène-anticorps: Reconnaissance des analogues décapeptidiques du fragment α67-76 du récepteur RACh par les anticorps anti-RACh
    • Cung, M. T., Marraud, M., Tsikaris, V., Sakarellos, C., Papadouli, I., and Tzartos, S. J. (1992) Etude par RMN-2D des interactions antigène- anticorps: reconnaissance des analogues décapeptidiques du fragment α67-76 du récepteur RACh par les anticorps anti-RACh, J. Chim. Phys. 89, 167-173.
    • (1992) J. Chim. Phys. , vol.89 , pp. 167-173
    • Cung, M.T.1    Marraud, M.2    Tsikaris, V.3    Sakarellos, C.4    Papadouli, I.5    Tzartos, S.J.6
  • 25
  • 27
    • 0026951903 scopus 로고
    • Gradient-tailored exitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. (1992) Gradient-tailored exitation for single-quantum NMR spectroscopy of aqueous solutions, J. Biol. NMR 2, 661-665.
    • (1992) J. Biol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 28
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A., and Davis, D. G. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy, J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 29
    • 0037463033 scopus 로고    scopus 로고
    • NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors
    • Meyer, B., and Peters, T. (2003) NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors, Angew. Chem., Int. Ed. Engl. 42, 864-890.
    • (2003) Angew. Chem., Int. Ed. Engl. , vol.42 , pp. 864-890
    • Meyer, B.1    Peters, T.2
  • 30
    • 0001342923 scopus 로고
    • Theory of the Time Dependent Transferred Nuclear Overhauser Effect: Applications to Structural Analysis of Ligand-Protein Complexes in Solution
    • Clore, G. M., and Gronenborn, A. M. (1983) Theory of the Time Dependent Transferred Nuclear Overhauser Effect: Applications to Structural Analysis of Ligand-Protein Complexes in Solution, J. Magn. Reson. 53, 423-442.
    • (1983) J. Magn. Reson. , vol.53 , pp. 423-442
    • Clore, G.M.1    Gronenborn, A.M.2
  • 31
    • 12644267957 scopus 로고
    • Buildup rates of the NOE measured by 2D Proton Magnetic Resonance Spectroscopy: Implication for studies of protein conformation
    • Kumar, A., Wagner, G., Ernst, R. R., and Wüthrich, K. (1981) Buildup rates of the NOE measured by 2D Proton Magnetic Resonance Spectroscopy: Implication for studies of protein conformation, J. Am. Chem. Soc. 103, 3654-3658.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 3654-3658
    • Kumar, A.1    Wagner, G.2    Ernst, R.R.3    Wüthrich, K.4
  • 32
    • 0043092240 scopus 로고    scopus 로고
    • NMR Studies of Carbohydrates and Carbohydrate-mimetic Peptides Recognized by an Anti-Group B Streptococcus Antibody
    • Johnson, M. A., Jaseja, M., Zou, W., Jennings, H. J., Copié, V., Pinto, B. M., and Pincus, S. H. (2003) NMR Studies of Carbohydrates and Carbohydrate-mimetic Peptides Recognized by an Anti-Group B Streptococcus Antibody, J. Biol. Chem. 278, 24740-24752.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24740-24752
    • Johnson, M.A.1    Jaseja, M.2    Zou, W.3    Jennings, H.J.4    Copié, V.5    Pinto, B.M.6    Pincus, S.H.7
  • 34
    • 0028399654 scopus 로고
    • Characteristic patterns of metabolites from selective two-dimensional proton NMR
    • Zwahlen, C., Vincent, S. J., Ziegler, A., and Bodenhausen, G. (1994) Characteristic patterns of metabolites from selective two-dimensional proton NMR, J. Magn. Reson., Ser. B 103, 299-302.
    • (1994) J. Magn. Reson., Ser. B , vol.103 , pp. 299-302
    • Zwahlen, C.1    Vincent, S.J.2    Ziegler, A.3    Bodenhausen, G.4
  • 36
    • 0037316363 scopus 로고    scopus 로고
    • ARIA: Automated assignment and NMR structure calculation
    • Linge, J. P., Habeck, M., Rieping, W., and Nilges, M. (2003) ARIA: automated assignment and NMR structure calculation, Bioinformatics 19, 315-316.
    • (2003) Bioinformatics , vol.19 , pp. 315-316
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 38
    • 0035859948 scopus 로고    scopus 로고
    • The Membrane-Proximal Tryptophan-Rich Region of the HIV Glycoprotein, gp41, Forms a Well-Defined Helix in Dodecylphosphocholine Micelles
    • Schibli, D. J., Monelero, R. C., and Vogel, H. J. (2001) The Membrane-Proximal Tryptophan-Rich Region of the HIV Glycoprotein, gp41, Forms a Well-Defined Helix in Dodecylphosphocholine Micelles, Biochemistry 40, 9570-9578.
    • (2001) Biochemistry , vol.40 , pp. 9570-9578
    • Schibli, D.J.1    Monelero, R.C.2    Vogel, H.J.3
  • 39
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 41
    • 0036165979 scopus 로고    scopus 로고
    • Epitope mapping of the O-chain polysaccharide of Legionella pneumophila serogroup 1 lipopolysaccharide by saturation-transfer-difference NMR spectroscopy
    • Kooistra, O., Herfurth, L., Luneberg, E., Frosch, M., Peters, T., and Zahringer, U. (2002) Epitope mapping of the O-chain polysaccharide of Legionella pneumophila serogroup 1 lipopolysaccharide by saturation-transfer-difference NMR spectroscopy, Eur. J. Biochem. 269, 573-582.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 573-582
    • Kooistra, O.1    Herfurth, L.2    Luneberg, E.3    Frosch, M.4    Peters, T.5    Zahringer, U.6
  • 42
    • 0000393431 scopus 로고
    • Theory and Applications of the Transferred Nuclear Overhauser Effect to the Study of the Conformations of Small Ligands Bound to Proteins
    • Clore, G. M., and Gronenborn, A. M. (1982) Theory and Applications of the Transferred Nuclear Overhauser Effect to the Study of the Conformations of Small Ligands Bound to Proteins, J. Magn. Reson. 48, 402-417.
    • (1982) J. Magn. Reson. , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2
  • 43
    • 0037732762 scopus 로고    scopus 로고
    • Solution Conformation of the Antibody-Bound Tyrosine Phosphorylation Site of the Nicotinic Acetylcholine Receptor β-Subunit in Its Phosphorylated and Nonphosphorylated States
    • Phan-Chan-Du, A., Hemmerlin, C., Krikorian, D., Sakarellos-Daitsiotis, M., Tsikaris, V., Sakarellos, C., Marinou, M., Thureau, A., Cung, M. T., and Tzartos, S. (2003) Solution Conformation of the Antibody-Bound Tyrosine Phosphorylation Site of the Nicotinic Acetylcholine Receptor β-Subunit in Its Phosphorylated and Nonphosphorylated States, Biochemistry 42, 7371-7380.
    • (2003) Biochemistry , vol.42 , pp. 7371-7380
    • Phan-Chan-Du, A.1    Hemmerlin, C.2    Krikorian, D.3    Sakarellos-Daitsiotis, M.4    Tsikaris, V.5    Sakarellos, C.6    Marinou, M.7    Thureau, A.8    Cung, M.T.9    Tzartos, S.10
  • 44
    • 0035873942 scopus 로고    scopus 로고
    • Structure of antibody-Bound Peptides and Retro-Inverso Analogues. A Transferred Nuclear Overhauser Effect Spectroscopy and Molecular Dynamics Approach
    • Phan-Chan-Du, A., Petit, M. C., Guichard, G., Briand, J. P., Muller, S., and Cung, M. T. (2001) Structure of antibody-Bound Peptides and Retro-Inverso Analogues. A Transferred Nuclear Overhauser Effect Spectroscopy and Molecular Dynamics Approach, Biochemistry 40, 5720-5727.
    • (2001) Biochemistry , vol.40 , pp. 5720-5727
    • Phan-Chan-Du, A.1    Petit, M.C.2    Guichard, G.3    Briand, J.P.4    Muller, S.5    Cung, M.T.6
  • 45
    • 0345791500 scopus 로고    scopus 로고
    • HIV-1 Vpu sequesters β-transducin repeat-containing protein (betaTrCP) in the cytoplasm and provokes the accumulation of β-catenin and other SCFbetaTrCP substrates
    • Besnard-Guerin, C., Belaidouni, N., Lassot, I., Segeral, E., Jobart, A., Marchal, C., and Benarous, R. (2004) HIV-1 Vpu sequesters β-transducin repeat-containing protein (betaTrCP) in the cytoplasm and provokes the accumulation of β-catenin and other SCFbetaTrCP substrates, J. Biol. Chem. 279, 788-795.
    • (2004) J. Biol. Chem. , vol.279 , pp. 788-795
    • Besnard-Guerin, C.1    Belaidouni, N.2    Lassot, I.3    Segeral, E.4    Jobart, A.5    Marchal, C.6    Benarous, R.7
  • 46
    • 0037756787 scopus 로고    scopus 로고
    • Structure of a β-TrCP1-Skp1-β-catenin complex: Destruction motif binding and lysine specificity of the SCF(β-TrCP1) ubiquitin ligase
    • Wu, G., Xu, G., Schulman, B. A., Jeffrey, P. D., Harper, J. W., and Pavletich, N. P. (2003) Structure of a β-TrCP1-Skp1-β-catenin complex: destruction motif binding and lysine specificity of the SCF(β-TrCP1) ubiquitin ligase, Mol. Cell 11, 1445-1456.
    • (2003) Mol. Cell , vol.11 , pp. 1445-1456
    • Wu, G.1    Xu, G.2    Schulman, B.A.3    Jeffrey, P.D.4    Harper, J.W.5    Pavletich, N.P.6
  • 48
    • 0030943906 scopus 로고    scopus 로고
    • Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution
    • Willbold, D., Hoffmann, S., and Rosch, P. (1997) Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution, Eur. J. Biochem. 245, 581-588.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 581-588
    • Willbold, D.1    Hoffmann, S.2    Rosch, P.3
  • 49
    • 0029977571 scopus 로고    scopus 로고
    • Solution structure of the cytoplasmic domain of human immunodeficiency virus type 1 encoded virus protein U (Vpu)
    • Federau, T., Schubert, U., Flossdorf, J., Henklein, P., Schomburg, D., and Wray, V. (1996) Solution structure of the cytoplasmic domain of human immunodeficiency virus type 1 encoded virus protein U (Vpu), Int. J. Pept. Protein Res. 47, 297-310.
    • (1996) Int. J. Pept. Protein Res. , vol.47 , pp. 297-310
    • Federau, T.1    Schubert, U.2    Flossdorf, J.3    Henklein, P.4    Schomburg, D.5    Wray, V.6
  • 50
    • 0034610348 scopus 로고    scopus 로고
    • Interaction of a Bacterially Expressed Peptide from the Receptor Binding Domain of Pseudomonas aeruginosa Pili Strain PAK with a Cross-Reactive Antibody: Conformation of the bound peptide
    • Campbell, P. A., Wong, W. Y., Irvin, R. T., and Sykes, B. D. (2000) Interaction of a Bacterially Expressed Peptide from the Receptor Binding Domain of Pseudomonas aeruginosa Pili Strain PAK with a Cross-Reactive Antibody: Conformation of the bound peptide, Biochemistry 39, 14847-14864.
    • (2000) Biochemistry , vol.39 , pp. 14847-14864
    • Campbell, P.A.1    Wong, W.Y.2    Irvin, R.T.3    Sykes, B.D.4
  • 51
    • 0017280973 scopus 로고
    • Phosphorylated sites in substrates of intracellular protein kinases. A common feature in amino acid sequences
    • Williams, R. E. (1976) phosphorylated sites in substrates of intracellular protein kinases. A common feature in amino acid sequences, Science 192, 473-474.
    • (1976) Science , vol.192 , pp. 473-474
    • Williams, R.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.