The zalpha domain of the editing enzyme dsRNA adenosine deaminase binds left-handed Z-RNA as well as Z-DNA.

Content Provider	Semantic Scholar
Author	Brown, Bernard Andrew Lowenhaupt, Ky Wilbert, Christina M. Hanlon, Eugene B. Rich, A.
Copyright Year	2000
Abstract	The Zalpha domain of human double-stranded RNA adenosine deaminase 1 binds specifically to left-handed Z-DNA and stabilizes the Z-conformation. Here we report spectroscopic and analytical results that demonstrate that Zalpha can also stabilize the left-handed Z-conformation in double-stranded RNA. Zalpha induces a slow transition from the right-handed A-conformation to the Z-form in duplex r(CG)(6), with an activation energy of 38 kcal mol(-1). We conclude that Z-RNA as well as Z-DNA can be accommodated in the tailored binding site of Zalpha. The specific binding of Z-RNA by Zalpha may be involved in targeting double-stranded RNA adenosine deaminase 1 for a role in hypermutation of RNA viruses.
Starting Page	281
Ending Page	302
Page Count	22
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.pnas.org/content/97/25/13532.full.pdf
PubMed reference number	11087828v1
Volume Number	97
Issue Number	25
Journal	Proceedings of the National Academy of Sciences of the United States of America
Language	English
Access Restriction	Open
Subject Keyword	Adenosine DNA, Z-Form Ligand Binding Domain RNA RNA, Double-Stranded kilocalorie
Content Type	Text
Resource Type	Article