Sandbox SRp20 John Davis
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==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=''> | ||
| - | SRp20 is one of the smallest members of Ser- and Arg-rich protein family. The RNA recognition motif (RRM)of SRp20 has a βαββαβ topology, with two α-helices packed against one side of the four-stranded β-sheet.<scene name='60/602705/Entire_rrm/1'>TextToBeDisplayed</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 RRM. TAP binds to the Arg-rich end of the protein that is opposite the RRM. So, RNA binds to one end of the protein, and TAP binds to the other. | + | SRp20 is one of the smallest members of Ser- and Arg-rich protein family. The RNA recognition motif (RRM)of SRp20 has a βαββαβ topology, with two α-helices packed against one side of the four-stranded β-sheet.<scene name='60/602705/Entire_rrm/1'>TextToBeDisplayed</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 RRM.<scene name='60/602705/Rna_and_rrm/1'>TextToBeDisplayed</scene> TAP binds to the Arg-rich end of the protein that is opposite the RRM. So, RNA binds to one end of the protein, and TAP binds to the other. |
== Function == | == Function == | ||
Revision as of 03:39, 14 October 2014
Structure
| |||||||||||
