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@article{710503, author = {Štefl, Richard and Allain, Frederic}, article_number = {5}, keywords = {ADENOSINE DEAMINASES; BACTERIOPHAGE-LAMBDA; CA2+ PERMEABILITY; RECEPTOR CHANNELS; BINDING DOMAIN; RECOGNITION; COMPLEX; ACT; TETRALOOPS;}, language = {eng}, issn = {1355-8382}, journal = {RNA}, title = {A novel RNA pentaloop fold involved in targeting ADAR2}, volume = {11}, year = {2005} }
TY - JOUR ID - 710503 AU - Štefl, Richard - Allain, Frederic PY - 2005 TI - A novel RNA pentaloop fold involved in targeting ADAR2 JF - RNA VL - 11 IS - 5 SP - 592-597 EP - 592-597 SN - 13558382 KW - ADENOSINE DEAMINASES KW - BACTERIOPHAGE-LAMBDA KW - CA2+ PERMEABILITY KW - RECEPTOR CHANNELS KW - BINDING DOMAIN KW - RECOGNITION KW - COMPLEX KW - ACT KW - TETRALOOPS; N2 - Adenosine deaminases that act on RNA (ADARs) catalyze the site-specific conversion of adenosine to inosine in primary mRNA transcripts, thereby affecting coding potential of mature mRNAs. Structural determinants that define the adenosine moieties for specific ADARs-mediated deaminations are currently unknown. We report the solution structure of the central region of the human R/G stem-loop pre-mRNA, a natural ADAR2 substrate encoding the subunit B of the glutamate receptor (R/G site). The structure reveals that the GCU(A/C)A pentaloop that is conserved in mammals and birds adopts a novel fold. The fold is stabilized by a complex interplay of hydrogen bonds and stacking interactions. We propose that this new pentaloop structure is an important determinant of the R/G site recognition by ADAR2. ER -
ŠTEFL, Richard a Frederic ALLAIN. A novel RNA pentaloop fold involved in targeting ADAR2. \textit{RNA}. 2005, roč.~11, č.~5, s.~592-597. ISSN~1355-8382.
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