4r3h: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r3h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r3h RCSB], [http://www.ebi.ac.uk/pdbsum/4r3h PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r3h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r3h RCSB], [http://www.ebi.ac.uk/pdbsum/4r3h PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/YTDC1_HUMAN YTDC1_HUMAN]] RNA-binding protein that regulates alternative splice site selection.<ref>PMID:20167602</ref> | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 22:16, 25 December 2014
The crystal structure of an apo RNA binding proteinThe crystal structure of an apo RNA binding protein
Structural highlights
Function[YTDC1_HUMAN] RNA-binding protein that regulates alternative splice site selection.[1] Publication Abstract from PubMedN6-methyladenosine (m6A) is the most abundant internal modification of nearly all eukaryotic mRNAs and has recently been reported to be recognized by the YTH domain family proteins. Here we present the crystal structures of the YTH domain of YTHDC1, a member of the YTH domain family, and its complex with an m6A-containing RNA. Our structural studies, together with transcriptome-wide identification of YTHDC1-binding sites and biochemical experiments, not only reveal the specific mode of m6A-YTH binding but also explain the preferential recognition of the GG(m6A)C sequences by YTHDC1. Structural basis for selective binding of mA RNA by the YTHDC1 YTH domain.,Xu C, Wang X, Liu K, Roundtree IA, Tempel W, Li Y, Lu Z, He C, Min J Nat Chem Biol. 2014 Sep 21. doi: 10.1038/nchembio.1654. PMID:25242552[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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