Sandbox Reserved 1654: Difference between revisions

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== Structure ==
== Structure ==
All <scene name='86/868187/Zz/3'>CPEB proteins</scene> 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 two zinc binding sites and 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).
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<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
<StructureSection load='2m13' size='340' side='left' 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 :
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. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.