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Sandbox Reserved 1481

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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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Click the edit this page tab at the top. Save the page after each step, then edit it again.
Click the 3D button (when editing, above the wikitext box) to insert Jmol.
show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
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Crystal structure of the catalytic domains of Mettl3/Mettl14 complex
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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.

This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

1 Structural highlights of the METTL3/METTL14 complex
2 Modification processes
3 Function of the modification within the cell
4 Disease and problems triggered by unfunctionnal METTL3/METTL14 complex
5 Relevance

Structural highlights of the METTL3/METTL14 complex

[1]

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 [2]or the B chain [3] of the complex.

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

Function of the modification within the cell

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.

Disease and problems triggered by unfunctionnal METTL3/METTL14 complex

Relevance

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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]

↑ 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

[3]

[4]

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_1481"

@@ Line 1: / Line 1: @@
 {{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' />==
-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.
+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=''>
@@ Line 14: / Line 14: @@
 [http://www.rcsb.org/structure/5K7M]
-This complex is composed of two differents proteins.
+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.
-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.
-METTL3
+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 ==

Sandbox Reserved 1481

From Proteopedia

Revision as of 09:59, 27 December 2018

Crystal structure of the catalytic domains of Mettl3/Mettl14 complex
spinqualitylabelsall models
Insert caption here
Show:Asymmetric Unit Biological Assembly
Drag the structure with the mouse to rotate
Export Animated Image

Contents

Structural highlights of the METTL3/METTL14 complex

Modification processes

Function of the modification within the cell

Disease and problems triggered by unfunctionnal METTL3/METTL14 complex

Relevance

References

Views

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