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 . 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 . TAP binds to the 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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