Sandbox Reserved 1654

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== Disease ==
== Disease ==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 
== References ==
== References ==
<references/>
<references/>

Revision as of 13:14, 8 January 2021

This Sandbox is Reserved from 26/11/2020, through 26/11/2021 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1643 through Sandbox Reserved 1664.
To get started:
  • 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.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Contents

Cytplasmic Polyadenylation Element-binding Protein (CPEB)

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.

Structure

All CPEB proteins have a similar structure :

  • A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
  • A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
    • Zinc finger patterns [3]

Caption for this structure

Drag the structure with the mouse to rotate

About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. includes :

      • A (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
      • β-hairpin with (residues 525-527) and (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
      • An (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
      • A 310 (residues 550-552).
      • 2 zinc binding sites, the first one is composed of and the second is composed of .
    • RRMs patterns [4]


Function

Disease

References

  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. ↑ Merkel DJ, Wells SB, Hilburn BC, Elazzouzi F, Perez-Alvarado GC, Lee BM. The C-Terminal Region of Cytoplasmic Polyadenylation Element Binding Protein Is a ZZ Domain with Potential for Protein-Protein Interactions. J Mol Biol. 2013 Mar 13. pii: S0022-2836(13)00156-3. doi:, 10.1016/j.jmb.2013.03.009. PMID:23500490 doi:10.1016/j.jmb.2013.03.009
  4. ↑ Afroz T, Skrisovska L, Belloc E, Guillen-Boixet J, Mendez R, Allain FH. A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins. Genes Dev. 2014 Jul 1;28(13):1498-514. doi: 10.1101/gad.241133.114. PMID:24990967 doi:http://dx.doi.org/10.1101/gad.241133.114
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