2009
The molecular dynamics study of the RNA-binding domain of ADAR2 bound to dsRNA
PASULKA, Josef; Jaroslav KOČA a Richard ŠTEFLZákladní údaje
Originální název
The molecular dynamics study of the RNA-binding domain of ADAR2 bound to dsRNA
Název česky
The molecular dynamics study of the RNA-binding domain of ADAR2 bound to dsRNA
Autoři
PASULKA, Josef; Jaroslav KOČA a Richard ŠTEFL
Vydání
7th Discussions in Structural Molecular Biology Nove Hrady, 12 - 14 March 2009, 2009
Další údaje
Jazyk
angličtina
Typ výsledku
Konferenční abstrakt
Obor
Genetika a molekulární biologie
Stát vydavatele
Česká republika
Utajení
není předmětem státního či obchodního tajemství
Označené pro přenos do RIV
Ne
Organizační jednotka
Přírodovědecká fakulta
ISSN
Klíčová slova česky
molecular dynamics; RNA-binding motive; ADAR2; RNA recognition
Klíčová slova anglicky
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.
Česky
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.
Návaznosti
| GA204/08/1212, projekt VaV |
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| IAA401630903, projekt VaV |
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| LA08008, projekt VaV |
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| MSM0021622413, záměr |
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