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Volumn 108, Issue 33, 2011, Pages 13528-13533

Structural conservation of druggable Hot spots in protein - Protein interfaces

Author keywords

Fragment based drug discovery; Inhibitor design; Ligand binding site; Side chain adjustment

Indexed keywords

HPV TRANSCRIPTION FACTOR E2; INITIATION FACTOR 4E; INITIATION FACTOR 4G; NUCLEAR PROTEIN; PROTEIN BCL XL; PROTEIN MDM2; PROTEIN ZIPA; TRANSCRIPTION FACTOR E2A; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 80051966197     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1101835108     Document Type: Article
Times cited : (206)

References (46)
  • 1
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • DOI 10.1038/nature06526, PII NATURE06526
    • Wells J., McClendon C. (2007) Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 450:1001-1009. (Pubitemid 350273630)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 2
    • 33646567148 scopus 로고    scopus 로고
    • Between a rock and a hard place?
    • DOI 10.1038/nchembio0306-112, PII NCHEMBIO0306112
    • Whitty A., Kumaravel G. (2006) Between a rock and a hard place? Nat Chem Biol 2:112-118. (Pubitemid 44323856)
    • (2006) Nature Chemical Biology , vol.2 , Issue.3 , pp. 112-118
    • Whitty, A.1    Kumaravel, G.2
  • 3
    • 50249154886 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions
    • Berg T. (2008) Small-molecule inhibitors of protein-protein interactions. Curr Opin Drug Discov Devel 11:666-674.
    • (2008) Curr Opin Drug Discov Devel , vol.11 , pp. 666-674
    • Berg, T.1
  • 4
    • 58849145512 scopus 로고    scopus 로고
    • Predicting druggable binding sites at the protein-protein interface
    • Fuller J.C., Burgoyne N.J., Jackson R.M. (2009) Predicting druggable binding sites at the protein-protein interface. Drug Disc Today 14:155-161.
    • (2009) Drug Disc Today , vol.14 , pp. 155-161
    • Fuller, J.C.1    Burgoyne, N.J.2    Jackson, R.M.3
  • 6
    • 21044444449 scopus 로고    scopus 로고
    • Pocketome via comprehensive identification and classification of ligand binding envelopes
    • DOI 10.1074/mcp.M400159-MCP200
    • An J., Totrov M., Abagyan R. (2005) Pocketome via comprehensive identification and classification of ligand binding envelopes. Mol Cell Proteomics 4:752-761. (Pubitemid 40873004)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.6 , pp. 752-761
    • An, J.1    Totrov, M.2    Abagyan, R.3
  • 7
    • 33646757492 scopus 로고    scopus 로고
    • On the nature of cavities on protein surfaces: Application to the identification of drug-binding sites
    • DOI 10.1002/prot.20897
    • Nayal M., Honig B. (2006) On the nature of cavities on protein surfaces: Application to the identification of drug-binding sites. Proteins 63:892-906. (Pubitemid 43765141)
    • (2006) Proteins: Structure, Function and Genetics , vol.63 , Issue.4 , pp. 892-906
    • Nayal, M.1    Honig, B.2
  • 8
    • 33746076877 scopus 로고    scopus 로고
    • Effects of conformational dynamics on predicted protein druggability
    • DOI 10.1002/cmdc.200500013
    • Brown S.P., Hajduk P.J. (2006) Effects of conformational dynamics on predicted protein druggability. ChemMedChem 1:70-72. (Pubitemid 44104979)
    • (2006) ChemMedChem , vol.1 , Issue.1 , pp. 70-72
    • Brown, S.P.1    Hajduk, P.J.2
  • 9
    • 34547583152 scopus 로고    scopus 로고
    • Transient pockets on protein surfaces involved in protein-protein interaction
    • DOI 10.1021/jm070095g
    • Eyrisch S., Helms V. (2007) Transient pockets on protein surfaces involved in proteinprotein interaction. J Med Chem 50:3457-3464. (Pubitemid 47195455)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.15 , pp. 3457-3464
    • Eyrisch, S.1    Helms, V.2
  • 10
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T., Wells J.A. (1995) A hot spot of binding energy in a hormone-receptor interface. Science 267:383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 11
    • 17144373303 scopus 로고    scopus 로고
    • Druggability indices for protein targets derived from NMr-based screening data
    • DOI 10.1021/jm049131r
    • Hajduk P.J., Huth J.R., Fesik S.W. (2005) Druggability indices for protein targets derived from NMR-based screening data. J Med Chem 48:2518-2525. (Pubitemid 40516441)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.7 , pp. 2518-2525
    • Hajduk, P.J.1    Huth, J.R.2    Fesik, S.W.3
  • 12
    • 0029868304 scopus 로고    scopus 로고
    • Locating and characterizing binding sites on proteins
    • Mattos C., Ringe D. (1996) Locating and characterizing binding sites on proteins. Nat Biotechnol 14:595-599. (Pubitemid 26135122)
    • (1996) Nature Biotechnology , vol.14 , Issue.5 , pp. 595-599
    • Mattos, C.1    Ringe, D.2
  • 14
    • 33947658802 scopus 로고    scopus 로고
    • Identification of hot spots within druggable binding regions by computational solvent mapping of proteins
    • DOI 10.1021/jm061134b
    • Landon M.R., Lancia D.R., Jr, Yu J., Thiel S.C., Vajda S. (2007) Identification of hot spots within druggable binding sites of proteins by computational solvent mapping. J Med Chem 50:1231-1240. (Pubitemid 46496323)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.6 , pp. 1231-1240
    • Landon, M.R.1    Lancia Jr., D.R.2    Yu, J.3    Thiel, S.C.4    Vajda, S.5
  • 15
    • 61449104961 scopus 로고    scopus 로고
    • Fragment-based identification of druggable "hot spots" of proteins using Fourier domain correlation techniques
    • Brenke R., et al. (2009) Fragment-based identification of druggable "hot spots" of proteins using Fourier domain correlation techniques. Bioinformatics 25:621-627.
    • (2009) Bioinformatics , vol.25 , pp. 621-627
    • Brenke, R.1
  • 16
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford P.J. (1985) A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J Med Chem 28:849-875.
    • (1985) J Med Chem , vol.28 , pp. 849-875
    • Goodford, P.J.1
  • 17
    • 0025916872 scopus 로고
    • Functionality maps of binding sites: A multiple Copy simultaneous search method
    • Miranker A., Karplus M. (1991) Functionality maps of binding sites: A multiple Copy simultaneous search method. Proteins 11:29-34.
    • (1991) Proteins , vol.11 , pp. 29-34
    • Miranker, A.1    Karplus, M.2
  • 18
    • 38549150173 scopus 로고    scopus 로고
    • Novel druggable hot spots in avian influenza neuraminidase H5N1 revealed by computational solvent mapping of a reduced and representative receptor ensemble
    • DOI 10.1111/j.1747-0285.2007.00614.x
    • Landon M.R., et al. (2008) Novel druggable hot spots in avian influenza neuraminidase H5N1 revealed by computational solvent mapping of a reduced and representative receptor ensemble. Chem Biol Drug Des 71:106-116. (Pubitemid 351160979)
    • (2008) Chemical Biology and Drug Design , vol.71 , Issue.2 , pp. 106-116
    • Landon, M.R.1    Amaro, R.E.2    Baron, R.3    Ngan, C.H.4    Ozonoff, D.5    Andrew M.Cammon, J.6    Vajda, S.7
  • 19
    • 77952553431 scopus 로고    scopus 로고
    • Rational design of small-molecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication
    • Christ F., et al. (2010) Rational design of small-molecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication. Nat Chem Biol 6:442-448.
    • (2010) Nat Chem Biol , vol.6 , pp. 442-448
    • Christ, F.1
  • 20
    • 79961092776 scopus 로고    scopus 로고
    • Small molecule inhibition of the TNF family cytokine CD40 ligand through a subunit fracture mechanism
    • Silvian L.F., et al. (2011) Small molecule inhibition of the TNF family cytokine CD40 ligand through a subunit fracture mechanism. ACS Chem Biol 6:636-647.
    • (2011) ACS Chem Biol , vol.6 , pp. 636-647
    • Silvian, L.F.1
  • 22
    • 38849180436 scopus 로고    scopus 로고
    • Targeting the eukaryotic translation initiation factor 4E for cancer therapy
    • DOI 10.1158/0008-5472.CAN-07-5635
    • Graff J.R., Konicek B.W., Carter J.H., Marcusson E.G. (2008) Targeting the eukaryotic translation initiation factor 4E for cancer therapy. Cancer Res 68:631-634. (Pubitemid 351206735)
    • (2008) Cancer Research , vol.68 , Issue.3 , pp. 631-634
    • Graff, J.R.1    Konicek, B.W.2    Carter, J.H.3    Marcusson, E.G.4
  • 24
    • 79551648564 scopus 로고    scopus 로고
    • Reversing chemoresistance by small molecule inhibition of the translation initiation complex eIF4F
    • Cencic R., et al. (2011) Reversing chemoresistance by small molecule inhibition of the translation initiation complex eIF4F. Proc Natl Acad Sci USA 108:1046-1051.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 1046-1051
    • Cencic, R.1
  • 25
    • 20344387872 scopus 로고    scopus 로고
    • Structural Biology: The structure of interleukin-2 complexed with its alpha receptor
    • DOI 10.1126/science.1109745
    • Rickert M., Wang X., Boulanger M.J., Goriatcheva N., Garcia K.C. (2005) The structure of interleukin-2 complexed with its alpha receptor. Science 308:1477-1480. (Pubitemid 40791303)
    • (2005) Science , vol.308 , Issue.5727 , pp. 1477-1480
    • Rickert, M.1    Wang, X.2    Boulanger, M.J.3    Goriatcheva, N.4    Garcia, K.C.5
  • 32
    • 0033959744 scopus 로고    scopus 로고
    • MDM2 - Master regulator of the p53 tumor suppressor protein
    • DOI 10.1016/S0378-1119(99)00487-4, PII S0378111999004874
    • Momand J., Wu H., Dasgupta G. (2000) MDM2-master regulator of the p53 tumor suppressor protein. Gene 242:15-29. (Pubitemid 30064488)
    • (2000) Gene , vol.242 , Issue.1-2 , pp. 15-29
    • Momand, J.1    Wu, H.-H.2    Dasgupta, G.3
  • 35
    • 4043175756 scopus 로고    scopus 로고
    • The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2
    • DOI 10.1101/gad.1220104
    • Abbate E.A., Berger J.M., Botchan M.R. (2004) The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2. Genes Dev 18:1981-1996. (Pubitemid 39071580)
    • (2004) Genes and Development , vol.18 , Issue.16 , pp. 1981-1996
    • Abbate, E.A.1    Berger, J.M.2    Botchan, M.R.3
  • 37
    • 0034600952 scopus 로고    scopus 로고
    • The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography
    • Mosyak L., et al. (2000) The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography. EMBO J 19:3179-3191. (Pubitemid 30428197)
    • (2000) EMBO Journal , vol.19 , Issue.13 , pp. 3179-3191
    • Mosyak, L.1    Zhang, Y.2    Glasfeld, E.3    Haney, S.4    Stahl, M.5    Seehra, J.6    Somers, W.S.7
  • 40
    • 14944348527 scopus 로고    scopus 로고
    • A shape-based 3-D scaffold hopping method and its application to a bacterial protein-protein interaction
    • DOI 10.1021/jm040163o
    • Rush T.S., 3rd, Grant J.A., Mosyak L., Nicholls A. (2005) A shape-based 3-D scaffold hopping method and its application to a bacterial protein-protein interaction. J Med Chem 48:1489-1495. (Pubitemid 40364556)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.5 , pp. 1489-1495
    • Rush III, T.S.1    Grant, J.A.2    Mosyak, L.3    Nicholls, A.4
  • 41
    • 27744586067 scopus 로고    scopus 로고
    • Small-molecule inhibition of TNF-alpha
    • He M.M., et al. (2005) Small-molecule inhibition of TNF-alpha. Science 310:1022-1025.
    • (2005) Science , vol.310 , pp. 1022-1025
    • He, M.M.1
  • 42
    • 7944225979 scopus 로고    scopus 로고
    • Protein-protein interactions: Hot spots and structurally conserved residues often locate in completed pockets that preorganized in the unbound states: Hot spots and structurally conserved residues often locate in completed pockets that preorganized in the unbound statesImplications for docking
    • Li X., Keskin O., Ma B., Nussinov R., Liang J. (2004) Protein-protein interactions: Hot spots and structurally conserved residues often locate in completed pockets that preorganized in the unbound states: Hot spots and structurally conserved residues often locate in completed pockets that preorganized in the unbound statesImplications for docking. J Mol Biol 344:781-785.
    • (2004) J Mol Biol , vol.344 , pp. 781-785
    • Li, X.1    Keskin, O.2    Ma, B.3    Nussinov, R.4    Liang, J.5
  • 44
    • 0027160197 scopus 로고
    • Backbone-dependent rotamer library for proteins. Application to side-chain prediction
    • Dunbrack R.L., Karplus M. (1993) Backbone-dependent rotamer library for proteins. Application to side-chain prediction. J Mol Biol 230:543-574.
    • (1993) J Mol Biol , vol.230 , pp. 543-574
    • Dunbrack, R.L.1    Karplus, M.2
  • 46
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott O., Olson A.J. (2010) AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 31:455-461.
    • (2010) J Comput Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.