메뉴 건너뛰기




Volumn 3, Issue 6, 2008, Pages

Model for the peptide-free conformation of class II MHC proteins

Author keywords

[No Author keywords available]

Indexed keywords

HLA DM ANTIGEN; HLA DR1 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PHENYLALANINE; MONOCLONAL ANTIBODY; PEPTIDE;

EID: 48749111890     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0002403     Document Type: Article
Times cited : (55)

References (59)
  • 1
    • 17644370329 scopus 로고    scopus 로고
    • Cell biology of antigen processing in vitro and in vivo
    • Trombetta ES, Mellman I (2005) Cell biology of antigen processing in vitro and in vivo. Annu Rev Immunol 23: 975-1028.
    • (2005) Annu Rev Immunol , vol.23 , pp. 975-1028
    • Trombetta, E.S.1    Mellman, I.2
  • 2
    • 0036174635 scopus 로고    scopus 로고
    • Binding interactions between peptides and proteins of the class II major histocompatibility complex
    • McFarland BJ, Beeson C (2002) Binding interactions between peptides and proteins of the class II major histocompatibility complex. Med Res Rev 22: 168-203.
    • (2002) Med Res Rev , vol.22 , pp. 168-203
    • McFarland, B.J.1    Beeson, C.2
  • 3
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
    • Stern LJ, Brown JH, Jardetzky TS, Gorga JC, Urban RG, et al. (1994) Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 368: 215-221.
    • (1994) Nature , vol.368 , pp. 215-221
    • Stern, L.J.1    Brown, J.H.2    Jardetzky, T.S.3    Gorga, J.C.4    Urban, R.G.5
  • 4
    • 26244451774 scopus 로고    scopus 로고
    • Conformational isomers of a peptide-class II major histocompatibility complex
    • Lovitch SB, Unanue ER (2005) Conformational isomers of a peptide-class II major histocompatibility complex. Immunol Rev 207: 293-313.
    • (2005) Immunol Rev , vol.207 , pp. 293-313
    • Lovitch, S.B.1    Unanue, E.R.2
  • 6
    • 0347926117 scopus 로고    scopus 로고
    • Formation or two peptide/MHC II isomers is catalyzed differentially by HLA-DM
    • Belmares MP, Busch R, Meflins ED, McConnell HM (2003) Formation or two peptide/MHC II isomers is catalyzed differentially by HLA-DM. Biochemistry 42: 838-847.
    • (2003) Biochemistry , vol.42 , pp. 838-847
    • Belmares, M.P.1    Busch, R.2    Meflins, E.D.3    McConnell, H.M.4
  • 7
    • 0033548189 scopus 로고    scopus 로고
    • Conformational isomers of a class II MHC-peptide complex in solution
    • Schmitt L, Boniface JJ, Davis MM, McConnell HM (1999) Conformational isomers of a class II MHC-peptide complex in solution. J Mol Biol 286: 207-218.
    • (1999) J Mol Biol , vol.286 , pp. 207-218
    • Schmitt, L.1    Boniface, J.J.2    Davis, M.M.3    McConnell, H.M.4
  • 8
    • 26244456282 scopus 로고    scopus 로고
    • Recognition of open conformers of classical MHC by chaperones and monoclonal antibodies
    • Hansen TH, Lybarger L, Yu L, Mitaksov V, Fremont DH (2005) Recognition of open conformers of classical MHC by chaperones and monoclonal antibodies. Immunol Rev 207: 100-111.
    • (2005) Immunol Rev , vol.207 , pp. 100-111
    • Hansen, T.H.1    Lybarger, L.2    Yu, L.3    Mitaksov, V.4    Fremont, D.H.5
  • 9
    • 0033522437 scopus 로고    scopus 로고
    • A conformational change in the human major histocompatibility complex protein HLA-DR1 induced by peptide binding
    • Zarutskie JA, Sato AK, Rushe MM, Chan IC, Lomakin A, et al. (1999) A conformational change in the human major histocompatibility complex protein HLA-DR1 induced by peptide binding. Biochemistry 38: 5878-5887.
    • (1999) Biochemistry , vol.38 , pp. 5878-5887
    • Zarutskie, J.A.1    Sato, A.K.2    Rushe, M.M.3    Chan, I.C.4    Lomakin, A.5
  • 10
    • 0034695675 scopus 로고    scopus 로고
    • Determinants of the peptide-induced conformational change in the human class II major histocompatibility complex protein HLA-DR1
    • Sato AK, Zarutskie JA, Rushe MM, Lomakin A, Natarajan SK, et al. (2000) Determinants of the peptide-induced conformational change in the human class II major histocompatibility complex protein HLA-DR1. J Biol Chem 275: 2165-2173.
    • (2000) J Biol Chem , vol.275 , pp. 2165-2173
    • Sato, A.K.1    Zarutskie, J.A.2    Rushe, M.M.3    Lomakin, A.4    Natarajan, S.K.5
  • 12
    • 0033559513 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate stability of HLA-DR1 complexes correlates with burial of hydrophobic residues in pocket 1
    • Natarajan SK, Stern LJ, Sadegh-Nasseri S (1999) Sodium dodecyl sulfate stability of HLA-DR1 complexes correlates with burial of hydrophobic residues in pocket 1. J Immunol 162: 3463-3470.
    • (1999) J Immunol , vol.162 , pp. 3463-3470
    • Natarajan, S.K.1    Stern, L.J.2    Sadegh-Nasseri, S.3
  • 13
    • 0034603779 scopus 로고    scopus 로고
    • A three-step kinetic mechanism for peptide binding to MHC class II proteins
    • Joshi RV, Zarutskie JA, Stern LJ (2000) A three-step kinetic mechanism for peptide binding to MHC class II proteins. Biochemistry 39: 3751-3762.
    • (2000) Biochemistry , vol.39 , pp. 3751-3762
    • Joshi, R.V.1    Zarutskie, J.A.2    Stern, L.J.3
  • 16
    • 11144356225 scopus 로고    scopus 로고
    • Monoclonal antibodies specific for the empty conformation of HLA-DR1 reveal aspects of the conformational change associated with peptide binding
    • Carven GJ, Chitta S, Hilgert I, Rushe MM, Baggio RF, et al. (2004) Monoclonal antibodies specific for the empty conformation of HLA-DR1 reveal aspects of the conformational change associated with peptide binding. J Biol Chem 279: 16561-16570.
    • (2004) J Biol Chem , vol.279 , pp. 16561-16570
    • Carven, G.J.1    Chitta, S.2    Hilgert, I.3    Rushe, M.M.4    Baggio, R.F.5
  • 17
    • 27144451208 scopus 로고    scopus 로고
    • Probing the ligand-induced conformational change in HLA-DR1 by selective chemical modification and mass spectrometric mapping
    • Carven GJ, Stern LJ (2005) Probing the ligand-induced conformational change in HLA-DR1 by selective chemical modification and mass spectrometric mapping. Biochemistry 44: 13625-13637.
    • (2005) Biochemistry , vol.44 , pp. 13625-13637
    • Carven, G.J.1    Stern, L.J.2
  • 18
    • 34848852941 scopus 로고    scopus 로고
    • Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations
    • Zheng W, Brooks BR, Thirumalai D (2007) Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations. Biophys J 93: 2289-2299.
    • (2007) Biophys J , vol.93 , pp. 2289-2299
    • Zheng, W.1    Brooks, B.R.2    Thirumalai, D.3
  • 19
    • 41649089359 scopus 로고    scopus 로고
    • Molecular dynamics simulations of hemoglobin A in different states and bound to DPG: Effector-linked perturbation of tertiary conformations and HbA concerted dynamics
    • Laberge M, Yonetani T (2008) Molecular dynamics simulations of hemoglobin A in different states and bound to DPG: effector-linked perturbation of tertiary conformations and HbA concerted dynamics. Biophys J 94: 2737-2751.
    • (2008) Biophys J , vol.94 , pp. 2737-2751
    • Laberge, M.1    Yonetani, T.2
  • 20
    • 0033084056 scopus 로고    scopus 로고
    • Empty and peptide-loaded class II major histocompatibility complex proteins produced by expression in Escherichia coli and folding in vitro
    • Frayser M, Sato AK, Xu L, Stern LJ (1999) Empty and peptide-loaded class II major histocompatibility complex proteins produced by expression in Escherichia coli and folding in vitro. Protein Expr Purif 15: 105-114.
    • (1999) Protein Expr Purif , vol.15 , pp. 105-114
    • Frayser, M.1    Sato, A.K.2    Xu, L.3    Stern, L.J.4
  • 21
    • 0033826815 scopus 로고    scopus 로고
    • A diverse set of oligomeric class II MHC-peptide complexes for probing T-cell receptor interactions
    • Cochran JR, Stern LJ (2000) A diverse set of oligomeric class II MHC-peptide complexes for probing T-cell receptor interactions. Chem Biol 7: 683-696.
    • (2000) Chem Biol , vol.7 , pp. 683-696
    • Cochran, J.R.1    Stern, L.J.2
  • 22
    • 0026571278 scopus 로고
    • The human class II MHC protein HLA-DR1 assembles as empty alpha beta heterodimers in the absence of antigenic peptide
    • Stern LJ, Wiley DC (1992) The human class II MHC protein HLA-DR1 assembles as empty alpha beta heterodimers in the absence of antigenic peptide. Cell 68: 465-477.
    • (1992) Cell , vol.68 , pp. 465-477
    • Stern, L.J.1    Wiley, D.C.2
  • 23
    • 4444256379 scopus 로고    scopus 로고
    • A hairpin turn in a class II MHC-bound peptide orients residues outside the binding groove for T cell recognition
    • Zavala-Ruiz Z, Strug I, Walker BD, Norris PJ, Stern LJ (2004) A hairpin turn in a class II MHC-bound peptide orients residues outside the binding groove for T cell recognition. Proc Natl Acad Sci U S A 101: 13279-13284.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 13279-13284
    • Zavala-Ruiz, Z.1    Strug, I.2    Walker, B.D.3    Norris, P.J.4    Stern, L.J.5
  • 24
    • 34249780547 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the native and partially folded states of ubiquitin: Influence of methanol cosolvent, pH, and temperature on the protein structure and dynamics
    • Kony DB, Hunenberger PH, van Gunsteren WF (2007) Molecular dynamics simulations of the native and partially folded states of ubiquitin: Influence of methanol cosolvent, pH, and temperature on the protein structure and dynamics. Protein Sci 16: 1101-1118.
    • (2007) Protein Sci , vol.16 , pp. 1101-1118
    • Kony, D.B.1    Hunenberger, P.H.2    van Gunsteren, W.F.3
  • 27
    • 0000388705 scopus 로고    scopus 로고
    • GEM, LINCS: A linear constraint solver for molecular simulations
    • Hess B, Bekker H, Berendsen HJC, FJ (1997) GEM, LINCS: A linear constraint solver for molecular simulations. J Comp Chem 18: 1463-1472.
    • (1997) J Comp Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen3    HJC, F.J.4
  • 28
    • 18744391399 scopus 로고    scopus 로고
    • Structural dynamics of the late repressor-DNA complex revealed by a multiscale simulation
    • Villa E, Balaeff A, Schulten K (2005) Structural dynamics of the late repressor-DNA complex revealed by a multiscale simulation. Proc Natl Acad Sci U S A 102: 6783-6788.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6783-6788
    • Villa, E.1    Balaeff, A.2    Schulten, K.3
  • 29
    • 0029633168 scopus 로고
    • GROMACS:A messeage-passing parallel molecular dynamic implementation
    • Berendsen HJC, van der Spoel D, van Drunen R (1995) GROMACS:A messeage-passing parallel molecular dynamic implementation. Comp Phys Comm 91: 43-56.
    • (1995) Comp Phys Comm , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    van der Spoel, D.2    van Drunen, R.3
  • 30
    • 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
  • 31
    • 5444264971 scopus 로고    scopus 로고
    • A polymorphic pocket at the P10 position contributes to peptide binding specificity in class II MHC proteins
    • Zavala-Ruiz Z, Strug I, Anderson MW, Gorski J, Stern LJ (2004) A polymorphic pocket at the P10 position contributes to peptide binding specificity in class II MHC proteins. Chem Biol 11: 1395-1402.
    • (2004) Chem Biol , vol.11 , pp. 1395-1402
    • Zavala-Ruiz, Z.1    Strug, I.2    Anderson, M.W.3    Gorski, J.4    Stern, L.J.5
  • 32
    • 0034084540 scopus 로고    scopus 로고
    • Objective comparison of protein structures: Error-scaled difference distance matrices
    • Schneider TR (2000) Objective comparison of protein structures: error-scaled difference distance matrices. Acta Cryst D56: 714-721.
    • (2000) Acta Cryst , vol.D56 , pp. 714-721
    • Schneider, T.R.1
  • 33
    • 2142661662 scopus 로고    scopus 로고
    • Dynamic flexibility of a peptide-binding groove of human HLA-DR1 class II MHC molecules: Normal mode analysis of the antigen peptide-class II MHC complex
    • Nojima H, Takeda-Shitaka M, Kurihara Y, Kamiya K, Umeyama H (2003) Dynamic flexibility of a peptide-binding groove of human HLA-DR1 class II MHC molecules: normal mode analysis of the antigen peptide-class II MHC complex. Chem Pharm Bull (Tokyo) 51: 923-928.
    • (2003) Chem Pharm Bull (Tokyo) , vol.51 , pp. 923-928
    • Nojima, H.1    Takeda-Shitaka, M.2    Kurihara, Y.3    Kamiya, K.4    Umeyama, H.5
  • 35
    • 34447278825 scopus 로고    scopus 로고
    • TCR recognition of peptide/MHC class II complexes and superantigens
    • Sundberg EJ, Deng L, Mariuzza RA (2007) TCR recognition of peptide/MHC class II complexes and superantigens. Semin Immunol 19: 262-271.
    • (2007) Semin Immunol , vol.19 , pp. 262-271
    • Sundberg, E.J.1    Deng, L.2    Mariuzza, R.A.3
  • 36
    • 0041333127 scopus 로고    scopus 로고
    • Structural, energetic, and functional analysis of a protein-protein interface at distinct stages of affinity maturation
    • Sundberg EJ, Andersen PS, Schlievert PM, Karjalainen K, Mariuzza RA (2003) Structural, energetic, and functional analysis of a protein-protein interface at distinct stages of affinity maturation. Structure 11: 1151-1161.
    • (2003) Structure , vol.11 , pp. 1151-1161
    • Sundberg, E.J.1    Andersen, P.S.2    Schlievert, P.M.3    Karjalainen, K.4    Mariuzza, R.A.5
  • 37
    • 0033119268 scopus 로고    scopus 로고
    • Role of the T cell receptor alpha chain in stabilizing TCR-superantigen-MHC class II complexes
    • Andersen PS, Lavoie PM, Sekaly RP, Churchill H, Kranz DM, et al. (1999) Role of the T cell receptor alpha chain in stabilizing TCR-superantigen-MHC class II complexes. Immunity 10: 473-483.
    • (1999) Immunity , vol.10 , pp. 473-483
    • Andersen, P.S.1    Lavoie, P.M.2    Sekaly, R.P.3    Churchill, H.4    Kranz, D.M.5
  • 38
    • 0028177699 scopus 로고
    • HLA-DR alpha chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes
    • Fu XT, Karr RW (1991) HLA-DR alpha chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes. Hum Immunol 39: 253-260.
    • (1991) Hum Immunol , vol.39 , pp. 253-260
    • Fu, X.T.1    Karr, R.W.2
  • 39
    • 0034684671 scopus 로고    scopus 로고
    • HLA-DM recognizes the flexible conformation of major histocompatibility complex class II
    • Chou CL, Sadegh-Nasseri S (2000) HLA-DM recognizes the flexible conformation of major histocompatibility complex class II. J Exp Med 192: 1697-1706.
    • (2000) J Exp Med , vol.192 , pp. 1697-1706
    • Chou, C.L.1    Sadegh-Nasseri, S.2
  • 40
    • 0033120523 scopus 로고    scopus 로고
    • Stable peptide binding to MHC class II molecule is rapid and is determined by a receptive conformation shaped by prior association with low affinity peptides
    • Natarajan SK, Assadi M, Sadegh-Nasseri S (1999) Stable peptide binding to MHC class II molecule is rapid and is determined by a receptive conformation shaped by prior association with low affinity peptides. J Immunol 162: 4030-4036.
    • (1999) J Immunol , vol.162 , pp. 4030-4036
    • Natarajan, S.K.1    Assadi, M.2    Sadegh-Nasseri, S.3
  • 41
    • 0030959548 scopus 로고    scopus 로고
    • Stability of empty and peptide-loaded class II major histocompatibility complex molecules at neutral and endosomal PH: Comparison to class I proteins
    • Reich Z, Altman JD, Boniface JJ, Lyons DS, Kozono H, et al. (1997) Stability of empty and peptide-loaded class II major histocompatibility complex molecules at neutral and endosomal PH: comparison to class I proteins. Proc Natl Acad Sci U S A 94: 2495-2500.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2495-2500
    • Reich, Z.1    Altman, J.D.2    Boniface, J.J.3    Lyons, D.S.4    Kozono, H.5
  • 42
    • 0030068236 scopus 로고    scopus 로고
    • A structural transition in class II major histocompatibility complex proteins at mildly acidic pH
    • Runnels HA, Moore JC, Jensen PE (1996) A structural transition in class II major histocompatibility complex proteins at mildly acidic pH. J Exp Med 183: 127-136.
    • (1996) J Exp Med , vol.183 , pp. 127-136
    • Runnels, H.A.1    Moore, J.C.2    Jensen, P.E.3
  • 43
    • 0030030896 scopus 로고    scopus 로고
    • Evidence for a conformational change in a class II major histocompatibility complex molecule occurring in the same pH range where antigen binding is enhanced
    • Boniface JJ, Lyons DS, Wettstein DA, Allbritton NL, Davis MM (1996) Evidence for a conformational change in a class II major histocompatibility complex molecule occurring in the same pH range where antigen binding is enhanced. J Exp Med 183: 119-126.
    • (1996) J Exp Med , vol.183 , pp. 119-126
    • Boniface, J.J.1    Lyons, D.S.2    Wettstein, D.A.3    Allbritton, N.L.4    Davis, M.M.5
  • 44
    • 0027941809 scopus 로고
    • MHC class II function preserved by low-affinity peptide interactions preceding stable binding
    • Sadegh-Nasseri S, Stern LJ, Wiley DC, Germain RN (1994) MHC class II function preserved by low-affinity peptide interactions preceding stable binding. Nature 370: 647-650.
    • (1994) Nature , vol.370 , pp. 647-650
    • Sadegh-Nasseri, S.1    Stern, L.J.2    Wiley, D.C.3    Germain, R.N.4
  • 45
    • 0025013141 scopus 로고
    • Characterization of the specificity of peptide binding to four DR haplotypes
    • O'Sullivan D, Sidney J, Appella E, Walker L, Phillips L, et al. (1990) Characterization of the specificity of peptide binding to four DR haplotypes. J Immunol 145: 1799-1808.
    • (1990) J Immunol , vol.145 , pp. 1799-1808
    • O'Sullivan, D.1    Sidney, J.2    Appella, E.3    Walker, L.4    Phillips, L.5
  • 46
    • 0026706746 scopus 로고
    • Identification of a motif for HLA-DR1 binding peptides using M13 display libraries
    • Hammer J, Takacs B, Sinigaglia F (1992) Identification of a motif for HLA-DR1 binding peptides using M13 display libraries. J Exp Med 176: 1007-1013.
    • (1992) J Exp Med , vol.176 , pp. 1007-1013
    • Hammer, J.1    Takacs, B.2    Sinigaglia, F.3
  • 47
    • 0030458137 scopus 로고    scopus 로고
    • HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules
    • Denzin LK, Hammond C, Cresswell P (1996) HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules. J Exp Med 184: 2153-2165.
    • (1996) J Exp Med , vol.184 , pp. 2153-2165
    • Denzin, L.K.1    Hammond, C.2    Cresswell, P.3
  • 48
    • 0030978530 scopus 로고    scopus 로고
    • HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH
    • Kropshofer H, Arndt SO, Moldenhauer G, Hammerling GJ, Vogt AB (1997) HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH. Immunity 6: 293-302.
    • (1997) Immunity , vol.6 , pp. 293-302
    • Kropshofer, H.1    Arndt, S.O.2    Moldenhauer, G.3    Hammerling, G.J.4    Vogt, A.B.5
  • 49
  • 50
    • 33846952190 scopus 로고    scopus 로고
    • HLA-DM targets the hydrogen bond between the histidine at position beta81 and peptide to dissociate HLA-DR-peptide complexes
    • Narayan K, Chou CL, Kim A, Hartman IZ, Dalai S, et al. (2007) HLA-DM targets the hydrogen bond between the histidine at position beta81 and peptide to dissociate HLA-DR-peptide complexes. Nat Immunol 8: 92-100.
    • (2007) Nat Immunol , vol.8 , pp. 92-100
    • Narayan, K.1    Chou, C.L.2    Kim, A.3    Hartman, I.Z.4    Dalai, S.5
  • 51
    • 0027217789 scopus 로고
    • Three-dimensional structure of the human class II histocompatibility antigen HLA-DRI
    • Brown JH, Jardetzky TS, Gorga JC, Stern LJ, Urban RG, et al. (1993) Three-dimensional structure of the human class II histocompatibility antigen HLA-DRI. Nature 364: 33-39.
    • (1993) Nature , vol.364 , pp. 33-39
    • Brown, J.H.1    Jardetzky, T.S.2    Gorga, J.C.3    Stern, L.J.4    Urban, R.G.5
  • 52
    • 0031953508 scopus 로고    scopus 로고
    • Structural characterization of a soluble and partially folded class I major histocompatibility heavy chain/beta 2m heterodimer
    • Bouvier M, Wiley DC (1998) Structural characterization of a soluble and partially folded class I major histocompatibility heavy chain/beta 2m heterodimer. Nat Struct Biol 5: 377-384.
    • (1998) Nat Struct Biol , vol.5 , pp. 377-384
    • Bouvier, M.1    Wiley, D.C.2
  • 53
    • 0027074320 scopus 로고
    • Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule
    • Fahnestock ML, Tamir I, Narhi L, Bjorkman PJ (1992) Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule. Science 258: 1658-1662.
    • (1992) Science , vol.258 , pp. 1658-1662
    • Fahnestock, M.L.1    Tamir, I.2    Narhi, L.3    Bjorkman, P.J.4
  • 54
    • 33744960215 scopus 로고    scopus 로고
    • The crystal structure of H-2D)(b) complexed with a partial peptide epitope suggests a major histocampatibility complex class I assembly intermediate
    • Glithero A, Tormo J, Doering K, Kojima M, Jones EY, et al. (2006) The crystal structure of H-2D)(b) complexed with a partial peptide epitope suggests a major histocampatibility complex class I assembly intermediate. J Biol Chem 281: 12699-12704.
    • (2006) J Biol Chem , vol.281 , pp. 12699-12704
    • Glithero, A.1    Tormo, J.2    Doering, K.3    Kojima, M.4    Jones, E.Y.5
  • 55
    • 5044232231 scopus 로고    scopus 로고
    • Conformational flexibility of the MHC class I alpha1-alpha2 domain in peptide bound and free states: A molecular dynamics simulation study
    • Zacharias M, Springer S (2004) Conformational flexibility of the MHC class I alpha1-alpha2 domain in peptide bound and free states: a molecular dynamics simulation study. Biophys J 87: 2203-2214.
    • (2004) Biophys J , vol.87 , pp. 2203-2214
    • Zacharias, M.1    Springer, S.2
  • 56
    • 33846550599 scopus 로고    scopus 로고
    • Comparative molecular dynamics analysis of tapasin-dependent and -independent MHC class I alleles
    • Sieker F, Springer S, Zacharias M (2007) Comparative molecular dynamics analysis of tapasin-dependent and -independent MHC class I alleles. Protein Sci 16: 299-308.
    • (2007) Protein Sci , vol.16 , pp. 299-308
    • Sieker, F.1    Springer, S.2    Zacharias, M.3
  • 57
    • 0034214403 scopus 로고    scopus 로고
    • Peptide and peptide mimetic inhibitors of antigen presentation by HLA-DR class II MHC molecules. Design, structure-activity relationships, and X-ray crystal structures
    • Bolin DR, Swain AL, Sarabu R, Berthel SJ, Gillespie P, et al. (2000) Peptide and peptide mimetic inhibitors of antigen presentation by HLA-DR class II MHC molecules. Design, structure-activity relationships, and X-ray crystal structures. J Med Chem 13: 2135-2148.
    • (2000) J Med Chem , vol.13 , pp. 2135-2148
    • Bolin, D.R.1    Swain, A.L.2    Sarabu, R.3    Berthel, S.J.4    Gillespie, P.5
  • 59
    • 0033229975 scopus 로고    scopus 로고
    • Experimental assessment or differences between related protein crystal structures
    • Kleywegt GJ (1999) Experimental assessment or differences between related protein crystal structures. Acta Crystallogr D Biol Crystallogr 55: 1878-1884.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 1878-1884
    • Kleywegt, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.