Feline immunodeficiency virus (FIV) shares structural similarities with human immunodeficiency virus (HIV): the surface glycoprotein gp36 corresponds to the HIV gp41, which drives virus-host cell interactions and is targeted by the peptide entry inhibitor enfuvirtide. Following a similar drug design strategy for the development of an anti-FIV therapy, the present study investigates ^(627-646)gp36 NHR, a peptide sequence derived from a region of gp36 that was previously found to interfere with...
[NMR paper] Probing the Conformational Space of the Cannabinoid Receptor 2 and a Systematic Investigation of DNP-Enhanced MAS NMR Spectroscopy of Proteins in Detergent Micelles
Probing the Conformational Space of the Cannabinoid Receptor 2 and a Systematic Investigation of DNP-Enhanced MAS NMR Spectroscopy of Proteins in Detergent Micelles
Tremendous progress has been made in determining the structures of G-protein coupled receptors (GPCR) and their complexes in recent years. However, understanding activation and signaling in GPCRs is still challenging due to the role of protein dynamics in these processes. Here, we show how dynamic nuclear polarization (DNP)-enhanced magic angle spinning nuclear magnetic resonance in combination with a unique pair labeling...
nmrlearner
Journal club
0
09-19-2023 08:52 PM
[NMR paper] Complex peptide macrocycle optimization: combining NMR restraints with conformational analysis to guide structure-based and ligand-based design
Complex peptide macrocycle optimization: combining NMR restraints with conformational analysis to guide structure-based and ligand-based design
Systematic optimization of large macrocyclic peptide ligands is a serious challenge. Here, we describe an approach for lead-optimization using the PD-1/PD-L1 system as a retrospective example of moving from initial lead compound to clinical candidate. We show how conformational restraints can be derived by exploiting NMR data to identify low-energy solution ensembles of a lead compound. Such restraints can be used to focus conformational search for...
nmrlearner
Journal club
0
08-03-2023 11:27 PM
[NMR paper] NMR investigation of domain III of Dengue virus E protein: antibody binding modulates conformational exchange in the antigen.
NMR investigation of domain III of Dengue virus E protein: antibody binding modulates conformational exchange in the antigen.
Related Articles NMR investigation of domain III of Dengue virus E protein: antibody binding modulates conformational exchange in the antigen.
J Virol. 2015 Dec 4;
Authors: Moraes AH, Simonelli L, Pedotti M, Almeida FC, Varani L, Valente AP
Abstract
Domain III of Dengue virus E protein (DIII) participates in recognition of cell receptors and in structural rearrangements required for membrane fusion and...
nmrlearner
Journal club
0
12-08-2015 08:28 PM
[NMR paper] Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.
Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full.gif Related Articles Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.
Proc Natl Acad Sci U S A. 2015 Mar 17;112(11):3374-9
Authors: Deshmukh L, Ghirlando R, Clore GM
Abstract
Assembly and maturation of the human...
nmrlearner
Journal club
0
06-05-2015 01:57 PM
[NMR paper] NMR Structure of the Myristylated Feline Immunodeficiency Virus Matrix Protein.
NMR Structure of the Myristylated Feline Immunodeficiency Virus Matrix Protein.
Related Articles NMR Structure of the Myristylated Feline Immunodeficiency Virus Matrix Protein.
Viruses. 2015;7(5):2210-2229
Authors: Brown LA, Cox C, Baptiste J, Summers H, Button R, Bahlow K, Spurrier V, Kyser J, Luttge BG, Kuo L, Freed EO, Summers MF
Abstract
Membrane targeting by the Gag proteins of the human immunodeficiency viruses (HIV types-1 and -2) is mediated by Gag's N-terminally myristylated matrix (MA) domain and is dependent on...
nmrlearner
Journal club
0
05-06-2015 11:59 AM
NMR Studies of the Q5A, G6S Unmyristylated Feline Immunodeficiency Virus Matrix Protein
NMR Studies of the Q5A, G6S Unmyristylated Feline Immunodeficiency Virus Matrix Protein
Publication date: 28 January 2014
Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1</br>
Author(s): Vaughn R. Spurrier , Lola Brown , Michael Summers</br>
</br></br>
</br></br>
More...
nmrlearner
Journal club
0
01-29-2014 12:50 AM
[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...
nmrlearner
Journal club
0
08-22-2010 05:08 PM
[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...
Conformational analysis of a new peptide derived from feline immunodeficiency virus gp36 in SDS micelles: An NMR-MD based investigation
Linear Mode
