Unknown

Dataset Information

0

High-resolution structure of the Influenza A virus PB2cap binding domain illuminates the changes induced by ligand binding.


ABSTRACT: In the face of increasing drug resistance and the rapidly increasing necessity for practicality in clinical settings, drugs targeting different viral proteins are needed in order to control influenza A and B. A small molecule that tenaciously adheres to the PB2cap binding domain, part of the heterotrimeric RNA polymerase machinery of influenza A virus and influenza B virus, is a promising drug candidate. Understanding the anatomic behavior of PB2cap upon ligand binding will aid in the development of a more robust inhibitor. In this report, the anatomic behavior of the influenza A virus PB2cap domain is established by solving the crystal structure of native influenza A virus PB2cap at 1.52?Å resolution. By comparing it with the ligand-bound structure, the dissociation and rotation of the ligand-binding domain in PB2cap from the C-terminal domain is identified. This domain movement is present in many PB2cap structures, suggesting its functional relevance for polymerase activity.

SUBMITTER: Constantinides A 

PROVIDER: S-EPMC5947696 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

High-resolution structure of the Influenza A virus PB2cap binding domain illuminates the changes induced by ligand binding.

Constantinides Amanda A   Gumpper Ryan R   Severin Chelsea C   Luo Ming M  

Acta crystallographica. Section F, Structural biology communications 20180226 Pt 3


In the face of increasing drug resistance and the rapidly increasing necessity for practicality in clinical settings, drugs targeting different viral proteins are needed in order to control influenza A and B. A small molecule that tenaciously adheres to the PB2cap binding domain, part of the heterotrimeric RNA polymerase machinery of influenza A virus and influenza B virus, is a promising drug candidate. Understanding the anatomic behavior of PB2cap upon ligand binding will aid in the developmen  ...[more]

Similar Datasets

| S-EPMC6854094 | biostudies-literature
| S-EPMC2242466 | biostudies-literature
| S-EPMC2635866 | biostudies-literature
| S-EPMC2629220 | biostudies-literature
| S-EPMC3979659 | biostudies-literature
| S-EPMC3625259 | biostudies-literature
| S-EPMC2374005 | biostudies-literature
| S-EPMC2708881 | biostudies-literature
2018-10-26 | PXD005575 | Pride
| S-EPMC5303882 | biostudies-literature