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Adenosine deaminase z-alpha domain

Field	Value
Symbol	z-alpha
Name	Adenosine deaminase z-alpha domain
image	PDB 1xmk EBI.jpg
caption	Crystal structure of the zb domain from the RNA editing enzyme ADAR1
Pfam	PF02295
Pfam_clan	CL0123
InterPro	IPR000607
SCOP	1qgp

In molecular biology, the protein domain **Adenosine deaminase z-alpha domain ** refers to an evolutionary conserved protein domain. This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA-editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.

Function

Double-stranded RNA-specific adenosine deaminase (EC) converts multiple adenosines to inosines and creates I/U mismatched base pairs in double-helical RNA substrates without apparent sequence specificity. DRADA has been found to modify adenosines in AU-rich regions more frequently, probably due to the relative ease of melting A/U base pairs compared to G/C base pairs. The protein functions to modify viral RNA genomes, and may be responsible for hypermutation of certain negative-stranded viruses. DRADA edits the mRNAs for the glutamate receptor subunits by site-selective adenosine deamination. The DRADA repeat is also found in viral E3 proteins, which contain a double-stranded RNA-binding domain.

Examples

Genes encoding proteins containing this domain include ADAR and ZBP1.

References

(October 1999). "The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA". Proc. Natl. Acad. Sci. U.S.A..

Info: Wikipedia Source

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