5wop

High Resolution Structure of Mutant CA09-PB2cap

spinqualitylabelsall models 5wop, resolution 1.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wop is a 2 chain structure with sequence from Influenza A virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.52Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F4MEU3_9INFA Publication Abstract from PubMed 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 A 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. High-resolution structure of the Influenza A virus PB2cap binding domain illuminates the changes induced by ligand binding.,Constantinides A, Gumpper R, Severin C, Luo M Acta Crystallogr F Struct Biol Commun. 2018 Mar 1;74(Pt 3):122-127. doi:, 10.1107/S2053230X18000894. Epub 2018 Feb 26. PMID:29497014 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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