Targeting the lateral interactions of transmembrane domain 5 of Epstein-Barr virus latent membrane protein 1

Biochimica et Biophysica Acta - Biomembranes

Volumn 1818, Issue 9, 2012, Pages 2282-2289

  Wang, Xiaohui ^a   Saludes, Jonel P ^a   Zhao, Tina X ^a   Csakai, Adam ^a   Fiorini, Zeno ^a   Chavez, Sherry A ^a   Li, Jing ^b   Lee, Gui In ^c   Varga, Krisztina ^d   Yin, Hang ^a  

^a UNIVERSITY OF COLORADO   (United States)

^b PEKING UNION MEDICAL COLLEGE HOSPITAL   (China)

^c PENNSYLVANIA STATE UNIVERSITY   (United States)

^d UNIVERSITY OF WYOMING   (United States)

Author keywords

Epstein Barr virus; High throughput screen; Latent membrane protein 1; Protein protein interaction; Small molecule inhibitor; Transmembrane domain

Indexed keywords

LATENT MEMBRANE PROTEIN 1; NSC 259242; PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INHIBITION; EPSTEIN BARR VIRUS; EPSTEIN BARR VIRUS INFECTION; HUMAN; HUMAN CELL; INTRACELLULAR SIGNALING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING;

ANTIVIRAL AGENTS; CELL LINE, TUMOR; DOSE-RESPONSE RELATIONSHIP, DRUG; HERPESVIRUS 4, HUMAN; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, BIOLOGICAL; MODELS, CHEMICAL; MODELS, MOLECULAR; MODELS, STATISTICAL; MOLECULAR CONFORMATION; NF-KAPPA B; NITRIC OXIDE; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION; SPECTROMETRY, FLUORESCENCE; STILBAMIDINES; VIRAL MATRIX PROTEINS;

HUMAN HERPESVIRUS 4;

EID: 84861812319     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2012.05.013     Document Type: Article

References (22)

1. D.L. Sackett, D. Sept, Protein-protein interactions: making drug design second nature, Nat. Chem. 1 (2009) 596-597.
2. M.R. Arkin, J.A. Wells, Small-molecule inhibitors of protein-protein interactions: progressing towards the dream, Nat. Rev. Drug Discov. 3 (2004) 301-317. (Pubitemid 38499758)
3. A.J. Wilson, Inhibition of protein-protein interactions using designed molecules, Chem. Soc. Rev. 38 (2009) 3289-3300.
4. H. Yin, Exogenous agents that target transmembrane domains of proteins, Angew. Chem. Int. Ed Engl. 47 (2008) 2744-2752.
5. T.X. Zhao, A.J. Martinko, V.H. Le, J. Zhao, H. Yin, Development of agents that modulate protein-protein interactions in membranes, Curr. Pharm. Des. 16 (2010) 1055-1062.
6. F.J. Quintana, D. Gerber, I. Bloch, I.R. Cohen, Y. Shai, A structurally altered D,L-amino acid TCRalpha transmembrane peptide interacts with the TCRalpha and inhibits T-cell activation in vitro and in an animal model, Biochemistry 46 (2007) 2317-2325. (Pubitemid 46362406)
7. L. Richter, L.M. Munter, J. Ness, P.W. Hildebrand, M. Dasari, S. Unterreitmeier, B. Bulic, M. Beyermann, R. Gust, B. Reif, S. Weggen, D. Langosch, G. Multhaup, Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization, Proc. Natl. Acad. Sci. U. S. A. 107 (2010) 14597-14602.
8. L.S. Young, A.B. Rickinson, Epstein-Barr virus: 40 years on, Nat. Rev. Cancer 4 (2004) 757-768. (Pubitemid 39331148)
9. D.W. Sammond, C. Joce, R. Takeshita, S. McQuate, N. Ghosh, J.M. Martin, H. Yin, Transmembrane peptides used to investigate the homo-oligomeric interface and binding hot-spot of latent membrane protein 1, Biopolymers 95 (2011) 772-784.
10. C. Zscherp, R. Schlesinger, J. Tittor, D. Oesterhelt, J. Heberle, In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy, Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 5498-5503. (Pubitemid 29234646)
11. C. Joce, A. Wiener, H. Yin, Transmembrane domain oligomerization propensity determined by ToxR assay, J. Vis. Exp. (2011) e2721.
12. C. Joce, A.A. Wiener, H. Yin, Multi-Tox: application of the ToxR-transcriptional reporter assay to the study of multi-pass protein transmembrane domain oligomerization, Biochim. Biophys. Acta 1808 (2011) 2948-2953.
13. H. Yin, J.S. Slusky, B.W. Berger, R.S. Walters, G. Vilaire, R.I. Litvinov, J.D. Lear, G.A. Caputo, J.S. Bennett, W.F. DeGrado, Computational design of peptides that target transmembrane helices, Science 315 (2007) 1817-1822. (Pubitemid 46580135)
14. J. Cavanagh,W.J. Fairbrother, A.G. Palmer III.M. Rance, N.J. Skelton, Protein NMR Spectroscopy: Principles and Practice, 2nd ed. Academic Press, San Diego, CA, 2007.
15. P. Schanda, E. Kupce, B. Brutscher, SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds, J. Biomol. NMR 33 (2005) 199-211. (Pubitemid 43118574)
16. F. Delaglio, S. Grzesiek, G.W. Vuister, G. Zhu, J. Pfeifer, A. Bax, NMRPipe: a multi-dimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6 (1995) 277-293.
17. B.W. Jester, K.J. Cox, A. Gaj, C.D. Shomin, J.R. Porter, I. Ghosh, A coiled-coil enabled split-luciferase three-hybrid system: applied toward profiling inhibitors of protein kinases, J. Am. Chem. Soc. 132 (2010) 11727-11735.
18. T. Hessa, H. Kim, K. Bihlmaier, C. Lundin, J. Boekel, H. Andersson, I. Nilsson, S.H. White, G. von Heijne, Recognition of transmembrane helices by the endoplasmic reticulum translocon, Nature 433 (2005) 377-381. (Pubitemid 40203311)
19. D.S. Wishart, B.D. Sykes, F.M. Richards, Relationship between nuclear magnetic resonance chemical shift and protein secondary structure, J. Mol. Biol. 222 (1991) 311-333. (Pubitemid 121004009)
20. D.S. Wishart, B.D. Sykes, F.M. Richards, The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy, Biochemistry 31 (1992) 1647-1651.
21. D.S.Wishart, B.D. Sykes, The 13C chemical-shift index: a simplemethod for the identification of protein secondary structure using 13C chemical-shift data, J. Biomol. NMR 4 (1994) 171-180.
22. A. Rath, M. Glibowicka, V.G. Nadeau, G. Chen, C.M. Deber, Detergent binding explains anomalous SDS-PAGE migration of membrane proteins, Proc. Natl. Acad. Sci. U. S. A. 106 (2009) 1760-1765.