Related ArticlesNMR and molecular dynamics studies of an autoimmune myelin basic protein peptide and its antagonist: structural implications for the MHC II (I-Au)-peptide complex from docking calculations.
Eur J Biochem. 2004 Aug;271(16):3399-413
Authors: Tzakos AG, Fuchs P, van Nuland NA, Troganis A, Tselios T, Deraos S, Matsoukas J, Gerothanassis IP, Bonvin AM
Experimental autoimmune encephalomyelitis can be induced in susceptible animals by immunodominant determinants of myelin basic protein (MBP). To characterize the molecular features of antigenic sites important for designing experimental autoimmune encephalomyelitis suppressing molecules, we report structural studies, based on NMR experimental data in conjunction with molecular dynamic simulations, of the potent linear dodecapeptide epitope of guinea pig MBP, Gln74-Lys75-Ser76-Gln77-Arg78-Ser79-Gln80-Asp81-Glu82-Asn83-Pro84-Val85 [MBP(74-85)], and its antagonist analogue Ala81MBP(74-85). The two peptides were studied in both water and Me(2)SO in order to mimic solvent-dependent structural changes in MBP. The agonist MBP(74-85) adopts a compact conformation because of electrostatic interactions of Arg78 with the side chains of Asp81 and Glu82. Arg78 is 'locked' in a well-defined conformation, perpendicular to the peptide backbone which is practically solvent independent. These electrostatic interactions are, however, absent from the antagonist Ala81MBP(74-85), resulting in great flexibility of the side chain of Arg78. Sequence alignment of the two analogues with several species of MBP suggests a critical role for the positively charged residue Arg78, firstly, in the stabilization of the local microdomains (epitopes) of the integral protein, and secondly, in a number of post-translational modifications relevant to multiple sclerosis, such as the conversion of charged arginine residues to uncharged citrullines. Flexible docking calculations on the binding of the MBP(74-85) antigen to the MHC class II receptor site I-A(u) using haddock indicate that Gln74, Ser76 and Ser79 are MHC II anchor residues. Lys75, Arg78 and Asp81 are prominent, solvent-exposed residues and, thus, may be of importance in the formation of the trimolecular T-cell receptor-MBP(74-85)-MHC II complex.
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Biochim Biophys Acta. 2011 Aug;1808(8):2019-30
Authors: Romo TD, Bradney LA, Greathouse DV, Grossfield A
Abstract
One approach to the growing health problem of antibiotic resistant bacteria is the development of antimicrobial peptides (AMPs) as alternative treatments. The...
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Structure and Dynamics of the A?21–30 Peptide from the Interplay of NMR Experiments and Molecular Simulations
Structure and Dynamics of the A?21–30 Peptide from the Interplay of NMR Experiments and Molecular Simulations
Nicolas L. Fawzi, Aaron H. Phillips, Jory Z. Ruscio, Michaeleen Doucleff, David E. Wemmer and Teresa Head-Gordon
Journal of the American Chemical Society
DOI: 10.1021/ja204315n
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/bEQEah_ik60
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Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Chem Biol Drug Des. 2011 Feb 5;
Authors: Gizachew D, Dratz E
Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
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[NMR paper] Investigation of the interaction of myelin basic protein with phospholipid bilayers u
Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy.
Related Articles Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy.
Chem Phys Lipids. 2004 Nov;132(1):47-54
Authors: Pointer-Keenan CD, Lee DK, Hallok K, Tan A, Zand R, Ramamoorthy A
Interaction of bovine myelin basic protein and its constituent charge isomers (C1-C3) with phospholipid bilayers was studied using solid-state NMR experiments on model...
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[NMR paper] Proton NMR study of peptides from myelin basic protein: evidence for Lys74-His77 inte
Proton NMR study of peptides from myelin basic protein: evidence for Lys74-His77 interaction revealed from histidine line broadening.
Related Articles Proton NMR study of peptides from myelin basic protein: evidence for Lys74-His77 interaction revealed from histidine line broadening.
Biochim Biophys Acta. 1996 Mar 7;1293(1):23-30
Authors: Koshy KM, Hashim GA, Boggs JM
Residues 69-84 of guinea pig myelin basic protein contain the encephalitogenic determinant for the Lewis rat. Insertion of histidine and glycine at positions 77 and 78 in bovine...
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08-22-2010 02:27 PM
[NMR paper] Interaction of two complementary fragments of the bovine spinal cord myelin basic pro
Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phosphatidylglycerol bilayers, studied by 2H and 31P NMR spectroscopy.
Related Articles Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phosphatidylglycerol bilayers, studied by 2H and 31P NMR spectroscopy.
Biochemistry. 1993 Sep 21;32(37):9709-13
Authors: Hayer-Hartl M, Brophy PJ, Marsh D, Watts A
The interaction of two complementary fragments of myelin basic protein from bovine spinal cord with...
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[NMR paper] Interaction of myelin basic protein with single bilayers on a solid support: an NMR,
Interaction of myelin basic protein with single bilayers on a solid support: an NMR, DSC and polarized infrared ATR study.
Related Articles Interaction of myelin basic protein with single bilayers on a solid support: an NMR, DSC and polarized infrared ATR study.
Biochim Biophys Acta. 1993 Sep 19;1151(2):127-36
Authors: Reinl HM, Bayerl TM
The interaction of myelin basic protein (MBP) with single bilayers on a solid support (planar and spherical support) is studied by deuterium nuclear magnetic resonance (2H-NMR), differential scanning...
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Solid-State NMR Spectroscopy of Membrane-Associated Myelin Basic Protein-Conformation
Solid-State NMR Spectroscopy of Membrane-Associated Myelin Basic Protein-Conformation and Dynamics of an Immunodominant Epitope.
Related Articles Solid-State NMR Spectroscopy of Membrane-Associated Myelin Basic Protein-Conformation and Dynamics of an Immunodominant Epitope.
Biophys J. 2010 Aug 9;99(4):1247-1255
Authors: Ahmed MA, Bamm VV, Harauz G, Ladizhansky V
Myelin basic protein (MBP) maintains the tight multilamellar compaction of the myelin sheath in the central nervous system through peripheral binding of adjacent lipid bilayers of...