Sandbox Reserved 1481

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{{Sandbox_Reserved_ESBS}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
{{Sandbox_Reserved_ESBS}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
==Crystal structure of the catalytic domains of Mettl3/Mettl14 complex<Structure load='5K7M' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />==
==Crystal structure of the catalytic domains of Mettl3/Mettl14 complex<Structure load='5K7M' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name 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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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 modifications of RNAs molecules which plays a key role in several biological fonctions.
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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[http://www.rcsb.org/structure/5K7M]
[http://www.rcsb.org/structure/5K7M]
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This complex is composed of two differents proteins.
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This complex is composed of two differents proteins forming two distinct but linked subunit of the enzymatic complex/. Each of these two protein is coded by two differents genes. The mettl3 gene codes for the N6-adenosine-methyltransferase 70 kDa subunit, which is a 225 Amino acid chain, whereas the Mettl14 codes for the N6-adenosine-methyltransferase subunit METTL14, which is composed of 349 amino acids. Each of these two proteins are corresponding to the A [https://www.ncbi.nlm.nih.gov/protein/5K7M_A]or the B chain [https://www.ncbi.nlm.nih.gov/protein/5K7M_B] of the complex.
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The METTL3 is a 225 Amino acid chain, whereas the METTL14 is composed of 349 amino acids. Each of these two proteins are corresponding to the A or the B chain of the complex.
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METTL3
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Thanks to their primary amino acid sequences both A and B chains have some specific conserved domains directly linked to their function and functionning.
== Modification processes ==
== Modification processes ==

Revision as of 09:59, 27 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 complex

Insert caption here

Drag the structure with the mouse to rotate

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 modifications of RNAs molecules which plays a key role in several biological fonctions.

Caption for this structure

Drag the structure with the mouse to rotate

References

<Structural Basis for Cooperative Function of Mettl3 and Mettl14 Methyltransferases/>[1] <Structural basis of N(6)-adenosine methylation by the METTL3-METTL14 complex./>[2]

  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
  2. 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
[3]

[4]


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