User:Juliet Obi/Sandbox 1
From Proteopedia
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== Overview == | == Overview == | ||
| - | Bromodomain adjacent to zinc finger 1A (BAZ1A) is a protein in humans encoded by the BAZ1A gene. The protein encoded by the BAZ1A gene contains the accessory subunit of the ATP-dependent chromatin assembly factor (ACF), which is a member of the imitation switch (ISWI) family of chromatin remodeling complexes including BAZ1B, BAZ2A and BAZ2B. BAZ1A structure contains a plant homeodomain (PHD) zinc finger at the N-terminus, a bromodomain at the C-terminus, a | + | Bromodomain adjacent to zinc finger 1A (BAZ1A) is a protein in humans encoded by the BAZ1A gene. The protein encoded by the BAZ1A gene contains the accessory subunit of the ATP-dependent chromatin assembly factor (ACF), which is a member of the imitation switch (ISWI) family of chromatin remodeling complexes including BAZ1B, BAZ2A and BAZ2B. BAZ1A structure contains a plant homeodomain (PHD) zinc finger at the N-terminus, a bromodomain at the C-terminus, a WAC motif and a LH (leucine-rich helical domain) motif <ref>DOI 10.1006/geno.1999.6071</ref>. BAZ1A is also known as ACF1, WALp1, hACF1 or WCRF180 <ref>PMID:20033039</ref>. |
== BAZ1A function == | == BAZ1A function == | ||
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=== BAZ1A bromodomain histone-ligand recognition === | === BAZ1A bromodomain histone-ligand recognition === | ||
| - | BAZ1A bromodomain as well as BAZ1B a similar bromodomain family member, both have a conserved asparagine "anchor" residue which in functional bromodomains, hydrogen bonds with the carbonyl group of a bound acetyl-lysine ligand and it is crucial for the interaction. This suggests that BAZ1A and BAZ1B could potentially bind an acety-lysine ligand <ref>DOI 10.1016/j.str.2015.08.004</ref>. Also, BAZ1B has an hydrophobic valine "gatekeeper" residue which is found in the binding pockets of several acetyl-lysine binding bromodomains <ref>DOI 10.1016/j.cell.2012.02.013</ref>. Surprisingly, the BAZ1A bromodomain gatekeeper was found to be a non-canonical glutamic acid residue which was found to be compatible with the bromodomain fold through the solving of the crystal structure of BAZ1A bromodomain. The glutamic acid residue introduces a negative charge on the side of the supposed binding pocket of BAZ1A which reduces its affinity for acetylated histone ligands <ref>DOI 10.1038/s41467-017-00866-0</ref>. | + | BAZ1A bromodomain as well as BAZ1B a similar bromodomain family member, both have a conserved asparagine "anchor" residue which in functional bromodomains, hydrogen bonds with the carbonyl group of a bound acetyl-lysine ligand and it is crucial for the interaction. This suggests that BAZ1A and BAZ1B could potentially bind an acety-lysine ligand <ref>DOI 10.1016/j.str.2015.08.004</ref>. Also, BAZ1B has an hydrophobic valine "gatekeeper" residue which is found in the binding pockets of several acetyl-lysine binding bromodomains <ref>DOI 10.1016/j.cell.2012.02.013</ref>. Surprisingly, the BAZ1A bromodomain gatekeeper was found to be a non-canonical glutamic acid residue which was found to be compatible with the bromodomain fold through the solving of the crystal structure of BAZ1A bromodomain. The glutamic acid residue introduces a negative charge on the side of the supposed binding pocket of BAZ1A which reduces its affinity for acetylated histone ligands <ref name="s41467">DOI 10.1038/s41467-017-00866-0</ref>. |
=== BAZ1A-PHD binding to DNA === | === BAZ1A-PHD binding to DNA === | ||
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| + | The PHD finger of bromodomains serves as an epigenetic reader by recognizing the N-terminal histone H3 tail when it is methylated <ref>DOI 10.1016/j.tibs.2011.03.005</ref>. The function of BAZ1A-PHD, N-terminal to its bromodomain, is however unknown <ref name="s41467"/>. | ||
== Ligand-interaction domain == | == Ligand-interaction domain == | ||
Revision as of 04:12, 1 December 2017
Bromodomain Adjacent to Zinc Finger domain 1A
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