2010
The computational view inside the dynamical behavior of the RNA-binding motive
PASULKA, Josef; Jaroslav KOČA a Richard ŠTEFLZákladní údaje
Originální název
The computational view inside the dynamical behavior of the RNA-binding motive
Název česky
The computational view inside the dynamical behavior of the RNA-binding motive
Autoři
PASULKA, Josef; Jaroslav KOČA a Richard ŠTEFL
Vydání
8th Discussions in Structural Molecular Biology, Nove Hrady, March 18 - 20, 2010, 2010
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: 30. 12. 2010 11:55, Mgr. Josef Pasulka, Ph.D.
V originále
The members of an enzyme family known as ADARs (adenosine deaminases that act on RNA) play a crucial role in the RNA editing process in all organisms. ADARs target double-stranded regions of nuclear-encoded RNA (dsRNA). 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. We focus on the N-terminal non-catalytic domain ADAR2, which recognizes the dsRNA with A-C mismatches. Molecular dynamics (MD) techniques are capable of providing detailed insight into the motions that occur during molecular recognition and how motional properties change upon binding. MD and NMR techniques synergistically reinforce each other when applied to the same system. Our goal in this work is to explain the role of mismatches and their flexibility for the ADAR2-dsRNA complex.
Česky
The members of an enzyme family known as ADARs (adenosine deaminases that act on RNA) play a crucial role in the RNA editing process in all organisms. ADARs target double-stranded regions of nuclear-encoded RNA (dsRNA). 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. We focus on the N-terminal non-catalytic domain ADAR2, which recognizes the dsRNA with A-C mismatches. Molecular dynamics (MD) techniques are capable of providing detailed insight into the motions that occur during molecular recognition and how motional properties change upon binding. MD and NMR techniques synergistically reinforce each other when applied to the same system. Our goal in this work is to explain the role of mismatches and their flexibility for the ADAR2-dsRNA complex.
Návaznosti
| GA204/08/1212, projekt VaV |
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| GD301/09/H004, 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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