Related ArticlesHelical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packaging.
Protein Sci. 2005 Feb;14(2):375-86
Authors: Morellet N, Druillennec S, Lenoir C, Bouaziz S, Roques BP
Gag protein oligomerization, an essential step during virus assembly, results in budding of spherical virus particles. This process is critically dependent on the spacer p2, located between the capsid and the nucleocapsid proteins. P2 contributes also, in association with NCp7, to specific recognition of the HIV-1 packaging signal resulting in viral genome encapsidation. There is no structural information about the 20 last amino acids of the C-terminal part of capsid (CA[CTD]) and p2, in the molecular mechanism of Gag assembly. In this study the structure of a peptide encompassing the 14 residues of p2 with the upstream 21 residues and the downstream 13 residues was determined by (1)H NMR in 30% trifluoroethanol (TFE). The main structural motif is a well-defined amphipathic alpha-helix including p2, the seven last residues of the CA(CTD), and the two first residues of NCp7. Peptides containing the p2 domain have a strong tendency to aggregate in solution, as shown by gel filtration analyses in pure H(2)O. To take into account the aggregation phenomena, models of dimer and trimer formed through hydrophobic or hydrophilic interfaces were constructed by molecular dynamic simulations. Gel shift experiments demonstrate that the presence of at least p2 and the 13 first residues of NCp7 is required for RNA binding. A computer-generated model of the Gag polyprotein segment (282-434)Gag interacting with the packaging element SL3 is proposed, illustrating the importance of p2 and NCp7 in genomic encapsidation.
Structure and dynamics of the lipid modifications of a transmembrane ?-helical peptide determined by (2)H solid-state NMR spectroscopy.
Structure and dynamics of the lipid modifications of a transmembrane ?-helical peptide determined by (2)H solid-state NMR spectroscopy.
Structure and dynamics of the lipid modifications of a transmembrane ?-helical peptide determined by (2)H solid-state NMR spectroscopy.
Biochim Biophys Acta. 2010 Dec 28;
Authors: Penk A, Müller M, Scheidt HA, Langosch D, Huster D
The fusion of biological membranes is mediated by integral membrane proteins with ?-helical transmembrane segments. Additionally, those proteins are often modified by the covalent...
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[NMR paper] Validation of helical tilt angles in the solution NMR structure of the Z domain of St
Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data.
Related Articles Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data.
Protein Sci. 2004 Feb;13(2):549-54
Authors: Zheng D, Aramini JM, Montelione GT
Staphylococcal protein A (SpA) is a virulence factor from Staphylococcus aureus that is able to bind to...
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[NMR paper] Structure determination of a peptide model of the repeated helical domain in Samia cy
Structure determination of a peptide model of the repeated helical domain in Samia cynthia ricini silk fibroin before spinning by a combination of advanced solid-state NMR methods.
Related Articles Structure determination of a peptide model of the repeated helical domain in Samia cynthia ricini silk fibroin before spinning by a combination of advanced solid-state NMR methods.
J Am Chem Soc. 2003 Jun 18;125(24):7230-7
Authors: Nakazawa Y, Asakura T
Fibrous proteins unlike globular proteins, contain repetitive amino acid sequences, giving rise...
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11-24-2010 09:01 PM
[NMR paper] Synthesis and NMR solution structure of an alpha-helical hairpin stapled with two dis
Synthesis and NMR solution structure of an alpha-helical hairpin stapled with two disulfide bridges.
Related Articles Synthesis and NMR solution structure of an alpha-helical hairpin stapled with two disulfide bridges.
Protein Sci. 2000 May;9(5):942-55
Authors: Barthe P, Rochette S, Vita C, Roumestand C
Helical coiled-coils and bundles are some of the most common structural motifs found in proteins. Design and synthesis of alpha-helical motifs may provide interesting scaffolds that can be useful as host structures to display functional sites,...
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11-18-2010 09:15 PM
[NMR paper] A solid-state NMR index of helical membrane protein structure and topology.
A solid-state NMR index of helical membrane protein structure and topology.
Related Articles A solid-state NMR index of helical membrane protein structure and topology.
J Magn Reson. 2000 May;144(1):150-5
Authors: Marassi FM, Opella SJ
The secondary structure and topology of membrane proteins can be described by inspection of two-dimensional (1)H-(15)N dipolar coupling/(15)N chemical shift polarization inversion spin exchange at the magic angle spectra obtained from uniformly (15)N-labeled samples in oriented bilayers. The characteristic...
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[NMR paper] Solution structure of a de novo helical protein by 2D-NMR spectroscopy.
Solution structure of a de novo helical protein by 2D-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution structure of a de novo helical protein by 2D-NMR spectroscopy.
J Mol Biol. 1994 Feb 25;236(3):862-8
Authors: Kuroda Y, Nakai T, Ohkubo T
The de novo design of proteins represents a critical test for our knowledge of protein structure. However, no structure of a successfully designed protein has yet been reported. This paper reports the design...
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08-22-2010 03:33 AM
[NMR paper] Solution structure of a de novo helical protein by 2D-NMR spectroscopy.
Solution structure of a de novo helical protein by 2D-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution structure of a de novo helical protein by 2D-NMR spectroscopy.
J Mol Biol. 1994 Feb 25;236(3):862-8
Authors: Kuroda Y, Nakai T, Ohkubo T
The de novo design of proteins represents a critical test for our knowledge of protein structure. However, no structure of a successfully designed protein has yet been reported. This paper reports the design...
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08-22-2010 03:33 AM
[NMR paper] Helical structure and folding of subunit c of F1F0 ATP synthase: 1H NMR resonance ass
Helical structure and folding of subunit c of F1F0 ATP synthase: 1H NMR resonance assignments and NOE analysis.
Related Articles Helical structure and folding of subunit c of F1F0 ATP synthase: 1H NMR resonance assignments and NOE analysis.
Biochemistry. 1993 Nov 16;32(45):12167-77
Authors: Girvin ME, Fillingame RH
Subunit c of the H(+)-transporting F1F0 ATP synthase (EC 3.6.1.34) is thought to fold across the membrane as a hairpin of two alpha-helices and function as a key component of the H(+)-translocase of F0. We report here the initial...
Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p
Linear Mode
