User:Brian Boyle/Sandbox 1: Difference between revisions
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== '''BRPF1 Association with the MOZ HAT Complex''' == | == '''BRPF1 Association with the MOZ HAT Complex''' == | ||
The MOZ Histone Acetyltransferase Complex is a tetramer consisting of MEAF6, ING5, BRPF1 (or BRPF2/BRPF3) and MOZ (or MORF)<ref name="Klein" />. Within BRPF1, there are two non-chromatin-binding modules surrounding the PZP domain that are responsible for its association with the MOZ HAT Complex. On the N-terminal side of the PZP, lies the MOZ/MORF binding domain<ref name="Lalonde">PMID:24065767</ref>. On the other side of the PZP domain, there is a small module involved in binding to ING5 and MEAF6<ref name="Ullah">PMID:18794358</ref>. BRPF1 seems to be required for the formation of the MOZ HAT complex, as it acts as a bridge associating MOZ or MORF with ING5 and MEAF6<ref name ="Ullah" />. | The MOZ Histone Acetyltransferase Complex is a tetramer consisting of MEAF6, ING5, BRPF1 (or BRPF2/BRPF3) and MOZ (or MORF)<ref name="Klein" />. Within BRPF1, there are two non-chromatin-binding modules surrounding the PZP domain that are responsible for its association with the MOZ HAT Complex. On the N-terminal side of the PZP, lies the MOZ/MORF binding domain<ref name="Lalonde">PMID:24065767</ref>. On the other side of the PZP domain, there is a small module involved in binding to ING5 and MEAF6<ref name="Ullah">PMID:18794358</ref>. BRPF1 seems to be required for the formation of the MOZ HAT complex, as it acts as a bridge associating MOZ or MORF with ING5 and MEAF6<ref name ="Ullah" />. | ||
== '''Evolution Section''' == | |||
== '''Links to Human Disease''' == | == '''Links to Human Disease''' == | ||
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</StructureSection> | </StructureSection> | ||
== '''Available Structures''' == | |||
== '''References''' == | == '''References''' == | ||
<references/> | <references/> | ||