Sandbox SRp20 John Davis

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==Structure==
==Structure==
<StructureSection load='2i2y' size='340' side='right' caption='[[SRp20]], [[NMR_Ensembles_of_Models | 28 NMR models]]' scene=''>
<StructureSection load='2i2y' size='340' side='right' caption='[[SRp20]], [[NMR_Ensembles_of_Models | 28 NMR models]]' scene=''>
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SRp20 is one of the smallest members of Ser- and Arg-rich protein family, with 150 amino acids in the protein. The RNA recognition motif (RRM)of SRp20 has a βαββαβ topology, with two α-helices packed against one side of the four-stranded <scene name='60/602705/Entire_rrm/1'>β-sheet</scene>. The β-sheet surface has a large hydrophobic core with the amino acids Tyr, Phe, Trp, and Ala. The aromatic amino acid residues in the β-sheet are what cause the affinity of RNA for SRp20. When RNA binds to to SRp20, 3-8 nucleotides in the RNA bind to the four-stranded β-sheet in the <scene name='60/602705/Rrm/1'>RRM</scene>. TAP binds to the <scene name='60/602705/New_tap_site/1'>Arg-rich</scene> α-helices that are opposite the β-sheet in the RRM. So, RNA binds to one side of the RRM and TAP binds to the other.
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SRp20 is one of the smallest members of Ser- and Arg-rich protein family with 150 amino acids in the protein. The RNA recognition motif (RRM)of SRp20 has a βαββαβ topology, with two α-helices packed against one side of the four-stranded <scene name='60/602705/Entire_rrm/1'>β-sheet</scene>. The β-sheet surface has a large hydrophobic core with the aromatic amino acids Tyr, Phe, and Trp. The aromatic amino acid residues in the β-sheet are what cause the affinity of RNA for SRp20. When RNA binds to to SRp20, 3-8 nucleotides in the RNA bind to the four-stranded β-sheet in the <scene name='60/602705/Rrm/1'>RRM</scene>. TAP binds to the <scene name='60/602705/New_tap_site/1'>Arg-rich</scene> α-helices that are opposite the β-sheet in the RRM. So, RNA binds to one side of the RRM and TAP binds to the other.(1)
== Function ==
== Function ==
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<scene name='60/602705/Pyrimidines/1'>TextToBeDisplayed</scene>
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SRp20 is important for alternative RNA splicing. SRp20 can work with the C-terminal domain (CTD) of RNA pol II to remove exons from RNA after transcription. A mechanism for this has not been proposed, however it is clear that the CTD and SRp20 must be present in order for alternative splicing of some exons to occur. (2)
== Disease ==
== Disease ==
== Relevance ==
== Relevance ==
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== Structural highlights ==
 
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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.
 
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 05:44, 14 October 2014

Structure

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References

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