메뉴 건너뛰기




Volumn 5, Issue 2, 2010, Pages

Limitations of ab initio predictions of peptide binding to MHC class II molecules

Author keywords

[No Author keywords available]

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PROTEOME; EPITOPE; HLA A ANTIGEN; HLA ANTIGEN CLASS 2; HLA DRB1*0101 ANTIGEN, HUMAN; HLA-DRB1*0101 ANTIGEN, HUMAN; PEPTIDE;

EID: 77949494386     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0009272     Document Type: Article
Times cited : (44)

References (49)
  • 2
    • 33745584371 scopus 로고    scopus 로고
    • A community resource benchmarking predictions of peptide binding to MHC-I molecules
    • Peters B, Bui HH, Frankild S, Nielson M, Lundegaard C, et al. (2006) A community resource benchmarking predictions of peptide binding to MHC-I molecules. PLoS Comput Biol 2: e65.
    • (2006) PLoS Comput Biol , vol.2
    • Peters, B.1    Bui, H.H.2    Frankild, S.3    Nielson, M.4    Lundegaard, C.5
  • 3
    • 0031455540 scopus 로고    scopus 로고
    • A structure-based algorithm to predict potential binding peptides to MHC molecules with hydrophobic binding pockets
    • Altuvia Y, Sette A, Sidney J, Southwood S, Margalit H (1997) A structure-based algorithm to predict potential binding peptides to MHC molecules with hydrophobic binding pockets. Hum Immunol 58: 1-11.
    • (1997) Hum Immunol , vol.58 , pp. 1-11
    • Altuvia, Y.1    Sette, A.2    Sidney, J.3    Southwood, S.4    Margalit, H.5
  • 4
    • 7944235990 scopus 로고    scopus 로고
    • A structure-based approach for prediction of MHC-binding peptides
    • Altuvia Y, Margalit H (2004) A structure-based approach for prediction of MHC-binding peptides. Methods 34: 454-459.
    • (2004) Methods , vol.34 , pp. 454-459
    • Altuvia, Y.1    Margalit, H.2
  • 5
    • 33646058599 scopus 로고    scopus 로고
    • Ab initio prediction of peptide-MHC binding geometry for diverse class I MHC allotypes
    • Bordner AJ, Abagyan R (2006) Ab initio prediction of peptide-MHC binding geometry for diverse class I MHC allotypes. Proteins 63: 512-526.
    • (2006) Proteins , vol.63 , pp. 512-526
    • Bordner, A.J.1    Abagyan, R.2
  • 6
    • 33645034411 scopus 로고    scopus 로고
    • Structural prediction of peptides binding to MHC class I molecules
    • Bui HH, Schiewe AJ, von Grafenstein H, Haworth IS (2006) Structural prediction of peptides binding to MHC class I molecules. Proteins 63: 43-52.
    • (2006) Proteins , vol.63 , pp. 43-52
    • Bui, H.H.1    Schiewe, A.J.2    von Grafenstein, H.3    Haworth, I.S.4
  • 7
    • 1042301998 scopus 로고    scopus 로고
    • Predicting peptide binding to MHC pockets via molecular modeling, implicit solvation, and global optimization
    • Schafroth HD, Floudas CA (2004) Predicting peptide binding to MHC pockets via molecular modeling, implicit solvation, and global optimization. Proteins 54: 534-556.
    • (2004) Proteins , vol.54 , pp. 534-556
    • Schafroth, H.D.1    Floudas, C.A.2
  • 8
    • 30744455459 scopus 로고    scopus 로고
    • Structural prediction of peptides bound to MHC class I
    • Fagerberg T, Cerottini JC, Michielin O (2006) Structural prediction of peptides bound to MHC class I. J Mol Biol 356: 521-546.
    • (2006) J Mol Biol , vol.356 , pp. 521-546
    • Fagerberg, T.1    Cerottini, J.C.2    Michielin, O.3
  • 9
    • 3042697402 scopus 로고    scopus 로고
    • A novel predictive technique for the MHC class II peptide-binding interaction
    • Davies MN, Sansom CE, Beazley C, Moss DS (2003) A novel predictive technique for the MHC class II peptide-binding interaction. Mol Med 9: 220-225.
    • (2003) Mol Med , vol.9 , pp. 220-225
    • Davies, M.N.1    Sansom, C.E.2    Beazley, C.3    Moss, D.S.4
  • 10
    • 67449134820 scopus 로고    scopus 로고
    • Ranking of binding and nonbinding peptides to MHC class I molecules using inverse folding approach: Implications for vaccine design
    • Singh SP, Mishra BN (2008) Ranking of binding and nonbinding peptides to MHC class I molecules using inverse folding approach: Implications for vaccine design. Bioinformation 3: 72-82.
    • (2008) Bioinformation , vol.3 , pp. 72-82
    • Singh, S.P.1    Mishra, B.N.2
  • 11
    • 2942627444 scopus 로고    scopus 로고
    • Coupling in silico and in vitro analysis of peptide-MHC binding: A bioinformatic approach enabling prediction of superbinding peptides and anchorless epitopes
    • Doytchinova IA, Walshe VA, Jones NA, Gloster SE, Borrow P, et al. (2004) Coupling in silico and in vitro analysis of peptide-MHC binding: a bioinformatic approach enabling prediction of superbinding peptides and anchorless epitopes. J Immunol 172: 7495-7502.
    • (2004) J Immunol , vol.172 , pp. 7495-7502
    • Doytchinova, I.A.1    Walshe, V.A.2    Jones, N.A.3    Gloster, S.E.4    Borrow, P.5
  • 12
    • 51349122244 scopus 로고    scopus 로고
    • Shift-invariant adaptive double threading: Learning MHC II-peptide binding
    • Zaitlen N, Reyes-Gomez M, Heckerman D, Jojic N (2008) Shift-invariant adaptive double threading: learning MHC II-peptide binding. J Comput Biol 15: 927-942.
    • (2008) J Comput Biol , vol.15 , pp. 927-942
    • Zaitlen, N.1    Reyes-Gomez, M.2    Heckerman, D.3    Jojic, N.4
  • 14
    • 65549131038 scopus 로고    scopus 로고
    • The PickPocket method for predicting binding specificities for receptors based on receptor pocket similarities: Application to MHC-peptide binding
    • Zhang H, Lund O, Nielsen M (2009) The PickPocket method for predicting binding specificities for receptors based on receptor pocket similarities: application to MHC-peptide binding. Bioinformatics 25: 1293-1299.
    • (2009) Bioinformatics , vol.25 , pp. 1293-1299
    • Zhang, H.1    Lund, O.2    Nielsen, M.3
  • 15
    • 59449094834 scopus 로고    scopus 로고
    • NetMHCpan, a method for MHC class I binding prediction beyond humans
    • Hoof I, Peters B, Sidney J, Pedersen LE, Sette A, et al. (2009) NetMHCpan, a method for MHC class I binding prediction beyond humans. Immunogenetics 61: 1-13.
    • (2009) Immunogenetics , vol.61 , pp. 1-13
    • Hoof, I.1    Peters, B.2    Sidney, J.3    Pedersen, L.E.4    Sette, A.5
  • 16
    • 39549084433 scopus 로고    scopus 로고
    • NetMHCpan, a method for quantitative predictions of peptide binding to any HLA-A and -B locus protein of known sequence
    • Nielsen M, Lundegaard C, Blicher T, Lamberth K, Harndahl M, et al. (2007) NetMHCpan, a method for quantitative predictions of peptide binding to any HLA-A and -B locus protein of known sequence. PLoS One 2: e796.
    • (2007) PLoS One , vol.2
    • Nielsen, M.1    Lundegaard, C.2    Blicher, T.3    Lamberth, K.4    Harndahl, M.5
  • 17
    • 48249083459 scopus 로고    scopus 로고
    • Nielsen M, Lundegaard C, Blicher T, Peters B, Sette A, et al. (2008) Quantitative predictions of peptide binding to any HLA-DR molecule of known sequence: NetMHCIIpan. PLoS Comput Biol 4: e1000107.
    • Nielsen M, Lundegaard C, Blicher T, Peters B, Sette A, et al. (2008) Quantitative predictions of peptide binding to any HLA-DR molecule of known sequence: NetMHCIIpan. PLoS Comput Biol 4: e1000107.
  • 18
    • 0035989339 scopus 로고    scopus 로고
    • Prediction of promiscuous peptides that bind HLA class I molecules
    • Brusic V, Petrovsky N, Zhang G, Bajic VB (2002) Prediction of promiscuous peptides that bind HLA class I molecules. Immunol Cell Biol 80: 280-285.
    • (2002) Immunol Cell Biol , vol.80 , pp. 280-285
    • Brusic, V.1    Petrovsky, N.2    Zhang, G.3    Bajic, V.B.4
  • 19
    • 0043245780 scopus 로고    scopus 로고
    • Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes
    • Gohlke H, Kiel C, Case DA (2003) Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes. J Mol Biol 330: 891-913.
    • (2003) J Mol Biol , vol.330 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3
  • 20
    • 24344456625 scopus 로고    scopus 로고
    • Study of the insulin dimerization: Binding free energy calculations and per-residue free energy decomposition
    • Zoete V, Meuwly M, Karplus M (2005) Study of the insulin dimerization: binding free energy calculations and per-residue free energy decomposition. Proteins 61: 79-93.
    • (2005) Proteins , vol.61 , pp. 79-93
    • Zoete, V.1    Meuwly, M.2    Karplus, M.3
  • 21
    • 33847650393 scopus 로고    scopus 로고
    • Computational alanine scanning mutagenesis-an improved methodological approach
    • Moreira IS, Fernandes PA, Ramos MJ (2007) Computational alanine scanning mutagenesis-an improved methodological approach. J Comput Chem 28: 644-654.
    • (2007) J Comput Chem , vol.28 , pp. 644-654
    • Moreira, I.S.1    Fernandes, P.A.2    Ramos, M.J.3
  • 22
    • 34248562740 scopus 로고    scopus 로고
    • Comparison between computational alanine scanning and per-residue binding free energy decomposition for protein-protein association using MM-GBSA: Application to the TCR-p-MHC complex
    • Zoete V, Michielin O (2007) Comparison between computational alanine scanning and per-residue binding free energy decomposition for protein-protein association using MM-GBSA: application to the TCR-p-MHC complex. Proteins 67: 1026-1047.
    • (2007) Proteins , vol.67 , pp. 1026-1047
    • Zoete, V.1    Michielin, O.2
  • 23
    • 0033021020 scopus 로고    scopus 로고
    • Generation of tissue-specific and promiscuous HLA ligand databases using DNA microarrays and virtual HLA class II matrices
    • Sturniolo T, Bono E, Ding J, Raddrizzani L, Tuereci O, et al. (1999) Generation of tissue-specific and promiscuous HLA ligand databases using DNA microarrays and virtual HLA class II matrices. Nat Biotechnol 17: 555-561.
    • (1999) Nat Biotechnol , vol.17 , pp. 555-561
    • Sturniolo, T.1    Bono, E.2    Ding, J.3    Raddrizzani, L.4    Tuereci, O.5
  • 25
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, et al. (1998) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393: 648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5
  • 26
    • 70449646933 scopus 로고    scopus 로고
    • An autoinhibitory tyrosine motif in the cell-cycle-regulated Nek7 kinase is released through binding of Nek9
    • Richards MW, O'Regan L, Mas-Droux C, Blot JM, Cheung J, et al. (2009) An autoinhibitory tyrosine motif in the cell-cycle-regulated Nek7 kinase is released through binding of Nek9. Mol Cell 36: 560-570.
    • (2009) Mol Cell , vol.36 , pp. 560-570
    • Richards, M.W.1    O'Regan, L.2    Mas-Droux, C.3    Blot, J.M.4    Cheung, J.5
  • 27
    • 42949139524 scopus 로고    scopus 로고
    • Wang P, Sidney J, Dow C, Mothe B, Sette A, et al. (2008) A systematic assessment of MHC class II peptide binding predictions and evaluation of a consensus approach. PLoS Comput Biol 4: e1000048.
    • Wang P, Sidney J, Dow C, Mothe B, Sette A, et al. (2008) A systematic assessment of MHC class II peptide binding predictions and evaluation of a consensus approach. PLoS Comput Biol 4: e1000048.
  • 28
    • 0029018773 scopus 로고
    • Ranking potential binding peptides to MHC molecules by a computational threading approach
    • Altuvia Y, Schueler O, Margalit H (1995) Ranking potential binding peptides to MHC molecules by a computational threading approach. J Mol Biol 249: 244-250.
    • (1995) J Mol Biol , vol.249 , pp. 244-250
    • Altuvia, Y.1    Schueler, O.2    Margalit, H.3
  • 29
    • 0041620259 scopus 로고    scopus 로고
    • MHCPred: A server for quantitative prediction of peptide-MHC binding
    • Guan P, Doytchinova IA, Zygouri C, Flower DR (2003) MHCPred: A server for quantitative prediction of peptide-MHC binding. Nucleic Acids Res 31: 3621-3624.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3621-3624
    • Guan, P.1    Doytchinova, I.A.2    Zygouri, C.3    Flower, D.R.4
  • 30
    • 34547778364 scopus 로고    scopus 로고
    • Prediction of MHC class II binding affinity using SMM-align, a novel stabilization matrix alignment method
    • Nielsen M, Lundegaard C, Lund O (2007) Prediction of MHC class II binding affinity using SMM-align, a novel stabilization matrix alignment method. BMC Bioinformatics 8: 238.
    • (2007) BMC Bioinformatics , vol.8 , pp. 238
    • Nielsen, M.1    Lundegaard, C.2    Lund, O.3
  • 31
    • 33644550942 scopus 로고    scopus 로고
    • Amino-terminal flanking residues determine the conformation of a peptide-class II MHC complex
    • Lovitch SB, Pu Z, Unanue ER (2006) Amino-terminal flanking residues determine the conformation of a peptide-class II MHC complex. J Immunol 176: 2958-2968.
    • (2006) J Immunol , vol.176 , pp. 2958-2968
    • Lovitch, S.B.1    Pu, Z.2    Unanue, E.R.3
  • 32
    • 0035338992 scopus 로고    scopus 로고
    • Naturally processed HLA class II peptides reveal highly conserved immunogenic flanking region sequence preferences that reflect antigen processing rather than peptide-MHC interactions
    • Godkin AJ, Smith KJ, Willis A, Tejada-Simon MV, Zhang J, et al. (2001) Naturally processed HLA class II peptides reveal highly conserved immunogenic flanking region sequence preferences that reflect antigen processing rather than peptide-MHC interactions. J Immunol 166: 6720-6727.
    • (2001) J Immunol , vol.166 , pp. 6720-6727
    • Godkin, A.J.1    Smith, K.J.2    Willis, A.3    Tejada-Simon, M.V.4    Zhang, J.5
  • 33
    • 0032488962 scopus 로고    scopus 로고
    • An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction
    • Samudrala R, Moult J (1998) An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction. J Mol Biol 275: 895-916.
    • (1998) J Mol Biol , vol.275 , pp. 895-916
    • Samudrala, R.1    Moult, J.2
  • 34
    • 0043180474 scopus 로고    scopus 로고
    • PISCES: A protein sequence culling server
    • Wang G, Dunbrack RL, Jr. (2003) PISCES: a protein sequence culling server. Bioinformatics 19: 1589-1591.
    • (2003) Bioinformatics , vol.19 , pp. 1589-1591
    • Wang, G.1    Dunbrack Jr., R.L.2
  • 35
    • 0036145846 scopus 로고    scopus 로고
    • Statistical potentials for fold assessment
    • Melo F, Sanchez R, Sali A (2002) Statistical potentials for fold assessment. Protein Sci 11: 430-448.
    • (2002) Protein Sci , vol.11 , pp. 430-448
    • Melo, F.1    Sanchez, R.2    Sali, A.3
  • 36
    • 1642534609 scopus 로고    scopus 로고
    • An accurate, residue-level, pair potential of mean force for folding and binding based on the distance-scaled, ideal-gas reference state
    • Zhang C, Liu S, Zhou H, Zhou Y (2004) An accurate, residue-level, pair potential of mean force for folding and binding based on the distance-scaled, ideal-gas reference state. Protein Sci 13: 400-411.
    • (2004) Protein Sci , vol.13 , pp. 400-411
    • Zhang, C.1    Liu, S.2    Zhou, H.3    Zhou, Y.4
  • 37
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 41
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert J-P, Ciccotti G, Berendsen HJC (1977) Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. Journal of Computational Physics 23: 327-341.
    • (1977) Journal of Computational Physics , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 42
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • 33-38
    • Humphrey W, Dalke A, Schulten K (1996) VMD: visual molecular dynamics. J Mol Graph 14: 33-38, 27-38.
    • (1996) J Mol Graph , vol.14 , pp. 27-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 43
    • 0037079570 scopus 로고    scopus 로고
    • Computational alanine scanning of the 1:1 human growth hormone-receptor complex
    • Huo S, Massova I, Kollman PA (2002) Computational alanine scanning of the 1:1 human growth hormone-receptor complex. J Comput Chem 23: 15-27.
    • (2002) J Comput Chem , vol.23 , pp. 15-27
    • Huo, S.1    Massova, I.2    Kollman, P.A.3
  • 44
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B, Nicholls A (1995) Classical electrostatics in biology and chemistry. Science 268: 1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 45
    • 77949536208 scopus 로고    scopus 로고
    • Sidney J, Southwood S, Oseroff C, Del Guercio M, Grey H, et al. (1998) Measurement of MHC/peptide interactions by gel filtration. Current protocals in immunology. new york: John Wiley & Sons, Inc. pp 18.13.11-18.13.19.
    • Sidney J, Southwood S, Oseroff C, Del Guercio M, Grey H, et al. (1998) Measurement of MHC/peptide interactions by gel filtration. Current protocals in immunology. new york: John Wiley & Sons, Inc. pp 18.13.11-18.13.19.
  • 46
    • 0023890867 scopus 로고
    • Measuring the accuracy of diagnostic systems
    • Swets JA (1988) Measuring the accuracy of diagnostic systems. Science 240: 1285-1293.
    • (1988) Science , vol.240 , pp. 1285-1293
    • Swets, J.A.1
  • 49
    • 0020083498 scopus 로고
    • The meaning and use of the area under a receiver operating characteristic (ROC) curve
    • Hanley JA, McNeil BJ (1982) The meaning and use of the area under a receiver operating characteristic (ROC) curve. Radiology 143: 29-36.
    • (1982) Radiology , vol.143 , pp. 29-36
    • Hanley, J.A.1    McNeil, B.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.