User:Brian Boyle/Sandbox 1: Difference between revisions
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== '''Bromodomain Structure & Acetyllysine Recognition''' == | == '''Bromodomain Structure & Acetyllysine Recognition''' == | ||
Consistent with most bromodomains, the BRPF1 bromodomain consists of a four α-helical bundle. These helices are termed <scene name='91/910741/Helical_bundle/3'>αZ, αA, αB, and αC</scene> (from N to C terminus)<ref name="Lubula_2014">PMID:25281266</ref>. | Consistent with most bromodomains, the BRPF1 bromodomain consists of a four α-helical bundle. These helices are termed <scene name='91/910741/Helical_bundle/3'>αZ, αA, αB, and αC</scene> (from N to C terminus)<ref name="Lubula_2014">PMID:25281266</ref>. There are two loop motifs present in its structure. The ZA loop links together the αZ and αA helices, while the BC loop links αB and αC<ref name="Lubula_2014" />. | ||
The BRPF1 bromodomain has been shown to recognize and bind to various acetylated lysine marks on the N-terminal tails of histones tails <ref name="Glass1" />. Using isothermal titration calorimetry (ITC) experiments, it was found that the BRPF1 bromodomain preferentially binds to histone H4 acetylated at positions K5 ([[2rs9]]) and K12 ([[4qyd]]) as well as H2A at position K5 ([[4qyl]]) <ref name="Obi" />,<ref>PMID:24333487</ref>. Interestingly, the BRPF1 bromodomain has also been shown to bind di-acetylated histone peptides with high affinity, including H4K5acK8ac and H4K5acK12ac <ref name="Obi" />. Acetyllysine recognition is coordinated by a number of residues in the bromodomain's binding pocket. Using NMR chemical shift perturbation experiments, Glass et al. reported several <scene name='91/910741/Nmr_resi_h4_binding/1'>key residues</scene> involved in coordinating histone H4 ligands (I27, L34, E36, V37, N83, and I88)<ref name="Obi" />. Notably, asparagine 83 was among these. The interactions between the amide nitrogen of asparagine with the carbonyl of the acetyllysine group is conserved in all bromodomains and is necessary for binding to occur <ref name ="Obi" />,<ref name ="Lubula_2014" />. | The BRPF1 bromodomain has been shown to recognize and bind to various acetylated lysine marks on the N-terminal tails of histones tails <ref name="Glass1" />. Using isothermal titration calorimetry (ITC) experiments, it was found that the BRPF1 bromodomain preferentially binds to histone H4 acetylated at positions K5 ([[2rs9]]) and K12 ([[4qyd]]) as well as H2A at position K5 ([[4qyl]]) <ref name="Obi" />,<ref>PMID:24333487</ref>. Interestingly, the BRPF1 bromodomain has also been shown to bind di-acetylated histone peptides with high affinity, including H4K5acK8ac and H4K5acK12ac <ref name="Obi" />. Acetyllysine recognition is coordinated by a number of residues in the bromodomain's binding pocket. Using NMR chemical shift perturbation experiments, Glass et al. reported several <scene name='91/910741/Nmr_resi_h4_binding/1'>key residues</scene> involved in coordinating histone H4 ligands (I27, L34, E36, V37, N83, and I88)<ref name="Obi" />. Notably, asparagine 83 was among these. The interactions between the amide nitrogen of asparagine with the carbonyl of the acetyllysine group is conserved in all bromodomains and is necessary for binding to occur <ref name ="Obi" />,<ref name ="Lubula_2014" />. | ||
