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
Conference abstract
Field of Study
Genetics and molecular biology
Country of publisher
Czech Republic
Confidentiality degree
is not subject to a state or trade secret
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
Changed: 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 |
| ||
| IAA401630903, research and development project |
| ||
| LA08008, research and development project |
| ||
| MSM0021622413, plan (intention) |
|