[NMR paper] Recognition of N6-Methyladenosine by the YTHDC1 YTH Domain Studied by Molecular Dynamics and NMR Spectroscopy: The Role of Hydration
Recognition of N6-Methyladenosine by the YTHDC1 YTH Domain Studied by Molecular Dynamics and NMR Spectroscopy: The Role of Hydration
The YTH domain of YTHDC1 belongs to a class of protein "readers", recognizing the N6-methyladenosine (m?A) chemical modification in mRNA. Static ensemble-averaged structures revealed details of N6-methyl recognition via a conserved aromatic cage. Here, we performed molecular dynamics (MD) simulations along with nuclear magnetic resonance (NMR) and isothermal titration calorimetry (ITC) to examine how dynamics and solvent interactions contribute to the m?A...
[NMR paper] The Structure of Mouse Cytomegalovirus m04 Protein Obtained from Sparse NMR Data Reveals a Conserved Fold of the m02-m06 Viral Immune Modulator Family.
The Structure of Mouse Cytomegalovirus m04 Protein Obtained from Sparse NMR Data Reveals a Conserved Fold of the m02-m06 Viral Immune Modulator Family.
Related Articles The Structure of Mouse Cytomegalovirus m04 Protein Obtained from Sparse NMR Data Reveals a Conserved Fold of the m02-m06 Viral Immune Modulator Family.
Structure. 2014 Aug 6;
Authors: Sgourakis NG, Natarajan K, Ying J, Vogeli B, Boyd LF, Margulies DH, Bax A
Abstract
Immunoevasins are key proteins used by viruses to subvert host immune responses. Determining their...
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The Structure of Mouse Cytomegalovirus m04 Protein Obtained from Sparse NMR Data Reveals a Conserved Fold of the m02-m06 Viral Immune Modulator Family
The Structure of Mouse Cytomegalovirus m04 Protein Obtained from Sparse NMR Data Reveals a Conserved Fold of the m02-m06 Viral Immune Modulator Family
Publication date: Available online 7 August 2014
Source:Structure</br>
Author(s): Nikolaos*G. Sgourakis , Kannan Natarajan , Jinfa Ying , Beat Vogeli , Lisa*F. Boyd , David*H. Margulies , Ad Bax</br>
Immunoevasins are key proteins used by viruses to subvert host immune responses. Determining their high-resolution structures is key to understanding virus-host interactions toward the design of vaccines and other...
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08-07-2014 10:05 PM
[NMR paper] N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involveme
N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation.
Related Articles N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation.
Biochem J. 1998 Jun 1;332 ( Pt 2):439-49
Authors: Moore GR, Cox MC, Crowe D, Osborne MJ, Rosell FI, Bujons J, Barker PD, Mauk MR, Mauk AG
The reductively dimethylated derivatives of horse and yeast iso-1-ferricytochromes c have been prepared and characterized for use as NMR...
N6-methyladenosine modification of the 5? epsilon structure of the HBV pregenome RNA regulates its encapsidation by the viral core protein - pnas.org
Linear Mode
