1QGP

NMR STRUCTURE OF THE Z-ALPHA DOMAIN OF ADAR1, 15 STRUCTURES

Summary for 1QGP

• Entry DOI: 10.2210/pdb1qgp/pdb
• Descriptor: PROTEIN (DOUBLE STRANDED RNA ADENOSINE DEAMINASE) (1 entity in total)
• Functional Keywords: z-alpha-z-dna binding domain, rna-editing, z-dna recognition, adar1, helix- turn-helix, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P55265
• Total number of polymer chains: 1
• Total formula weight: 8609.83

Authors

Schade, M.,Turner, C.J.,Kuehne, R.,Schmieder, P.,Lowenhaupt, K.,Herbert, A.,Rich, A.,Oschkinat, H. (deposition date: 1999-05-03, release date: 1999-10-19, Last modification date: 2023-12-27)

Primary citation

Schade, M.,Turner, C.J.,Kuhne, R.,Schmieder, P.,Lowenhaupt, K.,Herbert, A.,Rich, A.,Oschkinat, H.
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.USA, 96:12465-12470, 1999

PubMed Abstract: Double-stranded RNA deaminase I (ADAR1) contains the Z-DNA binding domain Zalpha. Here we report the solution structure of free Zalpha and map the interaction surface with Z-DNA, confirming roles previously assigned to residues by mutagenesis. Comparison with the crystal structure of the (Zalpha)(2)/Z-DNA complex shows that most Z-DNA contacting residues in free Zalpha are prepositioned to bind Z-DNA, thus minimizing the entropic cost of binding. Comparison with homologous (alpha+beta)helix-turn-helix/B-DNA complexes suggests that binding of Zalpha to B-DNA is disfavored by steric hindrance, but does not eliminate the possibility that related domains may bind to both B- and Z-DNA.

PubMed: 10535945
DOI: 10.1073/pnas.96.22.12465

Experimental method

SOLUTION NMR