H2N2V1, PubMed, Checkpoint, bibRecord, 000115

Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding.

Identifieur interne : 000115 ( PubMed/Checkpoint ); précédent : 000114; suivant : 000116

Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding.

Auteurs : Yan Wu [République populaire de Chine] ; Guangrong Qin ; Feng Gao ; Yue Liu ; Christopher J. Vavricka ; Jianxun Qi ; Hualiang Jiang ; Kunqian Yu ; George F. Gao

Source :

Scientific reports [ 2045-2322 ] ; 2013.

RBID : pubmed:23531861

Descripteurs français

KwdFr :
- Conception de médicament, Conformation des protéines (), Oséltamivir (analogues et dérivés), Oséltamivir (pharmacologie), Sialidase (), Sialidase (antagonistes et inhibiteurs), Sialidase (génétique), Simulation de dynamique moléculaire, Simulation numérique, Sous-type H1N1 du virus de la grippe A (enzymologie), Sous-type H2N2 du virus de la grippe A (enzymologie), Sous-type H3N2 du virus de la grippe A (enzymologie), Séquence d'acides aminés.
MESH :
- analogues et dérivés : Oséltamivir.
- antagonistes et inhibiteurs : Sialidase.
- enzymologie : Sous-type H1N1 du virus de la grippe A, Sous-type H2N2 du virus de la grippe A, Sous-type H3N2 du virus de la grippe A.
- génétique : Sialidase.
- pharmacologie : Oséltamivir.
- Conception de médicament, Conformation des protéines, Sialidase, Simulation de dynamique moléculaire, Simulation numérique, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence, Computer Simulation, Drug Design, Influenza A Virus, H1N1 Subtype (enzymology), Influenza A Virus, H2N2 Subtype (enzymology), Influenza A Virus, H3N2 Subtype (enzymology), Molecular Dynamics Simulation, Neuraminidase (antagonists & inhibitors), Neuraminidase (chemistry), Neuraminidase (genetics), Oseltamivir (analogs & derivatives), Oseltamivir (pharmacology), Protein Conformation (drug effects).
MESH :
- chemical , analogs & derivatives : Oseltamivir.
- chemical , antagonists & inhibitors : Neuraminidase.
- chemical , chemistry : Neuraminidase.
- drug effects : Protein Conformation.
- enzymology : Influenza A Virus, H1N1 Subtype, Influenza A Virus, H2N2 Subtype, Influenza A Virus, H3N2 Subtype.
- chemical , genetics : Neuraminidase.
- chemical , pharmacology : Oseltamivir.
- Amino Acid Sequence, Computer Simulation, Drug Design, Molecular Dynamics Simulation.

Abstract

The recently discovered 150-cavity (formed by loop residues 147-152, N2 numbering) adjacent to the enzymatic active site of group 1 influenza A neuraminidase (NA) has introduced a novel target for the design of next-generation NA inhibitors. However, only group 1 NAs, with the exception of the 2009 pandemic H1N1 NA, possess a 150-cavity, and no 150-cavity has been observed in group 2 NAs. The role of the 150-cavity played in enzymatic activity and inhibitor binding is not well understood. Here, we demonstrate for the first time that oseltamivir carboxylate can induce opening of the rigid closed N2 150-loop and provide a novel mechanism for 150-loop movement using molecular dynamics simulations. Our results provide the structural and biophysical basis of the open form of 150-loop and illustrates that the inherent flexibility and the ligand induced flexibility of the 150-loop should be taken into consideration for future drug design.

DOI: 10.1038/srep01551
PubMed: 23531861

Affiliations:

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 000127
to stream PubMed, to step Curation: 000127

Links to Exploration step

pubmed:23531861

Le document en format XML

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<front><div type="abstract" xml:lang="en">The recently discovered 150-cavity (formed by loop residues 147-152, N2 numbering) adjacent to the enzymatic active site of group 1 influenza A neuraminidase (NA) has introduced a novel target for the design of next-generation NA inhibitors. However, only group 1 NAs, with the exception of the 2009 pandemic H1N1 NA, possess a 150-cavity, and no 150-cavity has been observed in group 2 NAs. The role of the 150-cavity played in enzymatic activity and inhibitor binding is not well understood. Here, we demonstrate for the first time that oseltamivir carboxylate can induce opening of the rigid closed N2 150-loop and provide a novel mechanism for 150-loop movement using molecular dynamics simulations. Our results provide the structural and biophysical basis of the open form of 150-loop and illustrates that the inherent flexibility and the ligand induced flexibility of the 150-loop should be taken into consideration for future drug design.</div>
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Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding.

Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding.

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