Related ArticlesSolution structures of human immunodeficiency virus type 1 (HIV-1) and moloney murine leukemia virus (MoMLV) capsid protein major-homology-region peptide analogs by NMR spectroscopy.
Eur J Biochem. 1998 Oct 1;257(1):69-77
Authors: Clish CB, Peyton DH, Barklis E
The capsid domain of retroviral Gag proteins possesses a single highly conserved subdomain termed the major homology region (MHR). While the mutagenesis of residues in the MHR will impair virus infectivity, the precise solution structure and function of the MHR is not known. To aid the structure/function characterization of the MHR, the structures of synthetic peptides encompassing the MHR of the human immunodeficiency virus type I (HIV-1) and Moloney murine leukemia virus (MoMLV) capsid proteins were investigated by several techniques. Homology-based secondary-structure prediction suggested that the HIV-1 and MoMLV peptides could form 50% and 38% alpha-helix, respectively. CD studies indicated that, in the presence of 50% trifluoroethanol, the HIV-1 peptide adopts an alpha-helical structure over half of its length, while the MoMLV peptide is over one third alpha-helix. Further analysis by 1H-NMR suggested that the C-terminal portion of the MHR of each virus forms a helix in aqueous solution. Distance-geometry structures of each peptide were calculated from NOE distance restraints and were refined by restrained molecular dynamics. The C-terminal halves of both peptides were observed to be in an alpha-helical conformation, while the N-terminal halves were disordered. Furthermore, both helices were amphipathic with high conservation of amino acid side-chain character, suggesting that a conserved helical MHR C-terminus is essential to retroviral capsid protein function.
[NMR paper] NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine
NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine leukemia virus and the single-stranded pentanucleotide d(ACGCC): comparison with HIV-NCp7 complexes.
Related Articles NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine leukemia virus and the single-stranded pentanucleotide d(ACGCC): comparison with HIV-NCp7 complexes.
Biochemistry. 1999 Oct 5;38(40):12984-94
Authors: Schüler W, Dong C, Wecker K, Roques BP
The structure of the 56 amino acid nucleocapsid protein NCp10 of...
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[NMR paper] NMR solution structure of type II human cellular retinoic acid binding protein: impli
NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
Related Articles NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
Biochemistry. 1998 Sep 15;37(37):12727-36
Authors: Wang L, Li Y, Abildgaard F, Markley JL, Yan H
The structure of human apo-cellular retinoic acid binding protein II (apo-CRABPII) in solution at pH 7.3 has been determined by NMR spectroscopy. The sequential assignments of the 1H, 13C, and 15N resonances...
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[NMR paper] Comparison of the solution conformations of a human immunodeficiency virus peptidomim
Comparison of the solution conformations of a human immunodeficiency virus peptidomimetic and its retro-inverso isomer using 1H NMR spectroscopy.
Related Articles Comparison of the solution conformations of a human immunodeficiency virus peptidomimetic and its retro-inverso isomer using 1H NMR spectroscopy.
J Pept Res. 1997 Dec;50(6):421-35
Authors: Higgins KA, Bicknell W, Keah HH, Hearn MT
The solution conformations of the all L-alpha-peptide 1 and the corresponding retro-all D-alpha-peptide 2, two 20-metric peptides which generate antibodies...
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[NMR paper] NMR solution structure of the RNA-binding peptide from human immunodeficiency virus (
NMR solution structure of the RNA-binding peptide from human immunodeficiency virus (type 1) Rev.
Related Articles NMR solution structure of the RNA-binding peptide from human immunodeficiency virus (type 1) Rev.
Biochemistry. 1995 Jul 4;34(26):8242-9
Authors: Scanlon MJ, Fairlie DP, Craik DJ, Englebretsen DR, West ML
NMR spectroscopy has been used to solve the three-dimensional solution structure of a minimal RNA-binding domain of the Rev protein from the human immunodeficiency virus (type 1), an essential regulatory protein for viral...
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[NMR paper] NMR studies of a murine-human chimera of leukaemia inhibitory factor (LIF). Compariso
NMR studies of a murine-human chimera of leukaemia inhibitory factor (LIF). Comparison with human LIF.
Related Articles NMR studies of a murine-human chimera of leukaemia inhibitory factor (LIF). Comparison with human LIF.
Growth Factors. 1994;11(4):271-6
Authors: Maurer T, Smith DK, Owczarek CM, Layton MJ, Zhang JG, Nicola NA, Norton RS
Leukaemia inhibitory factor (LIF) is a polyfunctional cytokine active on many cell types. We present here 1H NMR studies on the solution properties and stability of MH35, a chimera of murine and human LIF...
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[NMR paper] Solution structure of human type-alpha transforming growth factor determined by heter
Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints.
Related Articles Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints.
Biochemistry. 1993 Jul 27;32(29):7334-53
Authors: Moy FJ, Li YC, Rauenbuehler P, Winkler ME, Scheraga HA, Montelione GT
Human type-alpha transforming growth factor (hTGF alpha) is a small mitogenic protein...
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[NMR paper] Solution structures of human transforming growth factor alpha derived from 1H NMR dat
Solution structures of human transforming growth factor alpha derived from 1H NMR data.
Related Articles Solution structures of human transforming growth factor alpha derived from 1H NMR data.
Biochemistry. 1990 Aug 28;29(34):7805-13
Authors: Kline TP, Brown FK, Brown SC, Jeffs PW, Kopple KD, Mueller L
The 600-MHz 1H NMR spectrum of the des-Val-Val mutant of human transforming growth factor alpha (TGF-alpha) was reassigned at pH = 6.3. The conformation space of des-Val-Val TGF-alpha was explored by distance geometry embedding followed by...