The solution structure of the Za domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA

Proceedings of the National Academy of Sciences of the United States of America

Volumn 96, Issue 22, 1999, Pages 12465-12470

  Schade, Markus ^a,c   Turner, Christopher J ^b   Kühne, Ronald ^c   Schmieder, Peter ^c   Lowenhaupt, Ky ^a   Herbert, Alan ^a   Rich, Alexander ^a   Oschkinat, Hartmut ^b  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^c LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DEAMINASE; DNA; DNA BINDING PROTEIN; DSRNA ADENOSINE DEAMINASE; DEAMINASE; DOUBLE STRANDED RNA;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; MOLECULAR GENETICS; NON-PROGRAMMATIC; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY; SOLUTION AND SOLUBILITY; CRYSTAL STRUCTURE; NUCLEAR OVERHAUSER EFFECT; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RNA EDITING; SEQUENCE ANALYSIS;

NON-PROGRAMMATIC;

ADENOSINE DEAMINASE; AMINO ACID SEQUENCE; BINDING SITES; DNA; DNA-BINDING PROTEINS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SOLUTIONS;

EID: 0033607056     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.96.22.12465     Document Type: Article

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