Sandbox Reserved 1654

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All CPEB proteins have a similar 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 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 which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
+
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** Zinc finger patterns
** Zinc finger patterns
<StructureSection load='2m13' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='2m13' size='340' side='right' caption='Caption for this structure' scene=''>
</StructureSection>
</StructureSection>
 +
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes :
 +
***A Rubredoxin turn (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
 +
***β-hairpin with β1 (residues 525-527) and β2 (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
 +
***An α1 helix (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 3<sub>10 helical turn (residues 550-552).
 +
***2 zinc binding sites, the first one is composed of Cys515, Cys518, Cys537, Cys540 and the second is composed of Cys527, Cys532, His545 and His553.
 +
** RRMs patterns
** RRMs patterns

Revision as of 18:32, 3 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 which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
    • Zinc finger patterns

Caption for this structure

Drag the structure with the mouse to rotate

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

      • A Rubredoxin turn (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
      • β-hairpin with β1 (residues 525-527) and β2 (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
      • An α1 helix (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 helical turn (residues 550-552).
      • 2 zinc binding sites, the first one is composed of Cys515, Cys518, Cys537, Cys540 and the second is composed of Cys527, Cys532, His545 and His553.
    • RRMs patterns


Function

Disease

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

  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
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