Sandbox Reserved 1654: Difference between revisions

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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 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

</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

Sandbox Reserved 1654: Difference between revisions

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@@ Line 7: / Line 7: @@
 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 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
 <StructureSection load='2m13' size='340' side='right' caption='Caption for this structure' scene=''>
 </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