Detailed Information on Publication Record
2009
The molecular dynamics study of the RNA-binding domain of ADAR2 bound to dsRNA
PASULKA, Josef, Jaroslav KOČA and Richard ŠTEFLBasic information
Original name
The molecular dynamics study of the RNA-binding domain of ADAR2 bound to dsRNA
Name in Czech
The molecular dynamics study of the RNA-binding domain of ADAR2 bound to dsRNA
Authors
PASULKA, Josef, Jaroslav KOČA and Richard ŠTEFL
Edition
7th Discussions in Structural Molecular Biology Nove Hrady, 12 - 14 March 2009, 2009
Other information
Language
English
Type of outcome
Konferenční abstrakt
Field of Study
Genetics and molecular biology
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
Organization unit
Faculty of Science
ISSN
Keywords (in Czech)
molecular dynamics; RNA-binding motive; ADAR2; RNA recognition
Keywords in English
molecular dynamics; RNA-binding motive; ADAR2; RNA recognition
Změněno: 10/4/2010 11:13, prof. RNDr. Jaroslav Koča, DrSc.
V originále
Like RNA splicing, RNA editing alters the sequence of an RNA from that encoded in the DNA. Typically, a single RNA splicing reaction removes a large block of contiguous sequence, whereas each RNA editing reaction changes only one or two nucleotides. Therefore splicing is a cut-and-paste mechanism whereas editing is one of fine-tuning. RNA editing by adenosine deamination is catalyzed by members of an enzyme family known as adenosine deaminases that act on RNA (ADARs). ADARs are RNA editing enzymes that target double-stranded regions of nuclear-encoded RNA. ADARs are also interesting in regard to the remarkable double-stranded structures of their substrates and how enzyme specificity is achieved with little regard to sequence. ADARs from all organisms have a common domain structure that includes variable numbers of double-stranded RNA (dsRNA) binding motifs (dsRBMs) followed by a highly conserved C-terminal catalytic domain. We focused on the N-terminal non-catalytic domain ADAR2, which recognizes the dsRNA with A-C mismatches. Using MD simulations, we study the role of mismatches and their flexibility for the formation of dsRBM-RNA complexes.
In Czech
Like RNA splicing, RNA editing alters the sequence of an RNA from that encoded in the DNA. Typically, a single RNA splicing reaction removes a large block of contiguous sequence, whereas each RNA editing reaction changes only one or two nucleotides. Therefore splicing is a cut-and-paste mechanism whereas editing is one of fine-tuning. RNA editing by adenosine deamination is catalyzed by members of an enzyme family known as adenosine deaminases that act on RNA (ADARs). ADARs are RNA editing enzymes that target double-stranded regions of nuclear-encoded RNA. ADARs are also interesting in regard to the remarkable double-stranded structures of their substrates and how enzyme specificity is achieved with little regard to sequence. ADARs from all organisms have a common domain structure that includes variable numbers of double-stranded RNA (dsRNA) binding motifs (dsRBMs) followed by a highly conserved C-terminal catalytic domain. We focused on the N-terminal non-catalytic domain ADAR2, which recognizes the dsRNA with A-C mismatches. Using MD simulations, we study the role of mismatches and their flexibility for the formation of dsRBM-RNA complexes.
Links
| GA204/08/1212, research and development project |
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| IAA401630903, research and development project |
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| LA08008, research and development project |
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| MSM0021622413, plan (intention) |
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