Peregrin: Difference between revisions
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== '''PWWP Domain''' == | == '''PWWP Domain''' == | ||
PWWP domains are a weakly conserved protein module that often contain a proline-tryptophan-tryptophan-proline motif and have been show to recognize methylated histones<ref name="chen">PMID:11836534</ref>. The BRPF1 PWWP domain has high selectivity for histone H3 Lys-36 ([[2x4w]]) that has been trimethylated (H3K36me3)<ref name="Vezzoli">PMID:20400950</ref>. The trimethyl mark at H3K36 has gained a lot attention due to its established roles is RNA splicing and developmental disorders<ref name="Paulina">PMID:19182803</ref>,<ref name="Nimura">PMID:19483677</ref>. Recognition of H3K36me3 is strongly dependent on the <scene name='91/910741/Pwwp_aromatic_cage/1'>aromatic cage</scene>, which consists of Tyr-1096, Tyr-1099, and Phe-1147. | PWWP domains are a weakly conserved protein module that often contain a proline-tryptophan-tryptophan-proline motif and have been show to recognize methylated histones<ref name="chen">PMID:11836534</ref>. The BRPF1 PWWP domain has high selectivity for histone H3 Lys-36 ([[2x4w]]) that has been trimethylated (H3K36me3)<ref name="Vezzoli">PMID:20400950</ref>. The trimethyl mark at H3K36 has gained a lot attention due to its established roles is RNA splicing and developmental disorders<ref name="Paulina">PMID:19182803</ref>,<ref name="Nimura">PMID:19483677</ref>. Recognition of H3K36me3 is strongly dependent on the <scene name='91/910741/Pwwp_aromatic_cage/1'>aromatic cage</scene>, which consists of Tyr-1096, Tyr-1099, and Phe-1147. Mutations of any of these aromatic residues abolishes all binding to the histone peptide<ref name="Vezzoli" />. | ||
</StructureSection> | </StructureSection> | ||