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. 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.
Function
Disease
Relevance
Structural highlights
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