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rdf:type |
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lifeskim:mentions |
umls-concept:C0014442,
umls-concept:C0037633,
umls-concept:C0043442,
umls-concept:C0086418,
umls-concept:C0162782,
umls-concept:C0205148,
umls-concept:C0678594,
umls-concept:C1167622,
umls-concept:C1382100,
umls-concept:C1412215,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
22
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pubmed:dateCreated |
1999-12-10
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-10090723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-10364558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-10518927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-1422145,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-1653449,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-1717158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-7527340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-8049221,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-8332212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-8520220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-8557047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-8662544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-8662853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-8674112,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-9153397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-9237992,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-9671561,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-9671809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-9697776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-9729788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-9748339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535945-9889202
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pubmed:keyword |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
96
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12465-70
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10535945-Adenosine Deaminase,
pubmed-meshheading:10535945-Amino Acid Sequence,
pubmed-meshheading:10535945-Binding Sites,
pubmed-meshheading:10535945-DNA,
pubmed-meshheading:10535945-DNA-Binding Proteins,
pubmed-meshheading:10535945-Humans,
pubmed-meshheading:10535945-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10535945-Models, Molecular,
pubmed-meshheading:10535945-Molecular Sequence Data,
pubmed-meshheading:10535945-Protein Conformation,
pubmed-meshheading:10535945-Sequence Homology, Amino Acid,
pubmed-meshheading:10535945-Solutions
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pubmed:year |
1999
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pubmed:articleTitle |
The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA.
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pubmed:affiliation |
Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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