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

Amanda Constantinides, Ryan Gumpper, Chelsea Severin, Ming Luo

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Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 authors.

Amanda ConstantinidesDepartment of Chemistry, Georgia State University, 50 Decatur Street, Atlanta, GA 30303, USA.ORCID 0000-0001-6470-606X

Ryan GumpperDepartment of Chemistry, Georgia State University, 50 Decatur Street, Atlanta, GA 30303, USA.ORCID 0000-0003-1309-3069

Chelsea SeverinDepartment of Chemistry, Georgia State University, 50 Decatur Street, Atlanta, GA 30303, USA.ORCID 0000-0003-4717-0608

Ming LuoDepartment of Chemistry, Georgia State University, 50 Decatur Street, Atlanta, GA 30303, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Amino Acid SequenceCatalytic DomainCrystallizationCrystallography, X-RayDNA-Directed RNA PolymerasesHumansInfluenza A virusLigandsModels, MolecularProtein ConformationViral ProteinsDNA-Directed RNA PolymerasesLigandsViral Proteinscap-snatchingdomain movementhigh resolution structuresInfluenza A viruspolymerase basic protein 2RNA polymerasetranscription

Identifiers

PMID29497014

DOI10.1107/S2053230X18000894

PMCPMC5947696

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