Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-37080
FEBS Lett 2007 Nov 13;58127:5300-6. doi: 10.1016/j.febslet.2007.10.025.
Show Gene links Show Anatomy links

Evidence that the C-terminal PB2-binding region of the influenza A virus PB1 protein is a discrete alpha-helical domain.

Poole EL , Medcalf L , Elton D , Digard P .


???displayArticle.abstract???
The influenza A virus RNA-dependent RNA polymerase is a heterotrimer composed of PB1, PB2 and PA subunits and essential for viral replication. However, little detailed structural information is available for this important enzyme. We show by circular dichroism spectroscopy that polypeptides from the C-terminus of PB1 that are capable of binding efficiently to PB2 fold into stable alpha-helical structures. Structure prediction analysis of this region of PB1 indicates that it likely consists of a three-helical bundle. Deletion of any of the helices abrogated transcriptional function. Thus, PB1 contains a C-terminal alpha-helical PB2-binding domain that is essential for nucleotide polymerization activity.

???displayArticle.pubmedLink??? 17967456
???displayArticle.link??? FEBS Lett
???displayArticle.grants??? [+]

Species referenced: Xenopus
Genes referenced: pbrm1