Sandbox Reserved 1481
From Proteopedia
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== Structural highlights of the METTL3/METTL14 complex== | == Structural highlights of the METTL3/METTL14 complex== | ||
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| + | [http://www.rcsb.org/structure/5K7M] | ||
== Modification processes == | == Modification processes == | ||
== Function of the modification within the cell == | == Function of the modification within the cell == | ||
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| + | Specific, and well controlled methylation of the nucleic acids is essential for proper gene regulation, whatever the studied organism or modification’s type. However the precise molecular role of m6A is unknown, it is knonw that for most mRNAs, m6A modification appear in long exons, near stop codons, and in 3′ UTRs and that this modification could influence mRNA stability, induce RNA conformational changes, modulate protein-RNA interactions, and even modify microRNA processing | ||
| + | One of the most prevalent modifications observed for mRNAs is N6-methyladenosine (m6A). Recent studies have intensely investigated how m6A-modification of RNA contributes to central events in biology. Nonfonctional m6A actors such as writers like METTL3 or METTL14, but also readers, and erasers are oftern linked to problems in self-renewal of stem cells, circadian clock and developmental defects, obesity, synaptic signaling, and cancers. | ||
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== Disease and problems triggered by unfunctionnal METTL3/METTL14 complex== | == Disease and problems triggered by unfunctionnal METTL3/METTL14 complex== | ||
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== References == | == References == | ||
| - | <Structural basis of N(6)-adenosine methylation by the METTL3-METTL14 complex./>[ | + | <Structural basis of N(6)-adenosine methylation by the METTL3-METTL14 complex./>[https://www.ncbi.nlm.nih.gov/pubmed/?term=27373337] |
<references/>[https://www.ncbi.nlm.nih.gov/pubmed/27281194] | <references/>[https://www.ncbi.nlm.nih.gov/pubmed/27281194] | ||
<references/>[https://www.ncbi.nlm.nih.gov/pubmed/27627798] | <references/>[https://www.ncbi.nlm.nih.gov/pubmed/27627798] | ||
<references/>[https://www.ncbi.nlm.nih.gov/pubmed/28121234] | <references/>[https://www.ncbi.nlm.nih.gov/pubmed/28121234] | ||
| - | <references/> | + | <references/> |
<references/> | <references/> | ||
Revision as of 16:18, 23 December 2018
| This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543. |
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Crystal structure of the catalytic domains of Mettl3/Mettl14 complexInsert caption here
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The complex METTL3/METTL14 is a heterodimer enzymatic complex involved into RNA post-transcription modifications. This complex is abble to add a methyl group on adenosin of the RNA, by catalyzing a m6(A) modification.The N(6)-methyladenosine (m(6)A) is a quite common, reversible chemical modification of functional RNAs which plays a key role in several biological fonctions.
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References
<Structural basis of N(6)-adenosine methylation by the METTL3-METTL14 complex./>[1]
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
