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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This is a default text for your page '''Sandbox SRp20 John Davis'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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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. 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.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Function ==
== Function ==

Revision as of 02:52, 14 October 2014

Structure

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References

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