WD repeat-containing protein: Difference between revisions

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<StructureSection load='2h9m' size='340' side='right' caption='Human WD-repeat protein 5 (grey) complex with histone H3 peptide (green) (PDB code [[2h9m]])'>
<StructureSection load='2h9m' size='340' side='right' caption='Human WD-repeat protein 5 (grey) complex with histone H3 peptide (green) (PDB code [[2h9m]])'>
== Function ==
== Function ==
'''WD-repeat protein 5''' (WDR5) contains 7 WD repeats. WD repeats are ca. 40 amino acid long usually bordered by Gly-His and Trp-Asp (WD).  WDR5 contributes to histone modification.  It may position the N-terminal of histone H3 for efficient methylation at Lys4.  This methylation is implicated in the control of activation of cell lineage genes during embryogenesis.  WDR5 interacts with histone-lysine N-methyltransferase (MLL)<ref>PMID:21531708</ref>.  WDR5 forms a beta propeller structure.
'''WD repeat-containing proteins''' (WDR) contain 4 or more repeating WD units. WD repeats are ca. 40 amino acid long usually bordered by Gly-His and Trp-Asp (WD).  All WDRs form a β-propeller structure.  WDRs have critical roles in many biological functions like signal transduction, transcription regulation and apoptosis<ref>PMID:11814058</ref>.  <br />
*'''WD-repeat protein 5''' (WDR5) contains 7 WD repeats.  WDR5 contributes to histone modification.  It may position the N-terminal of histone H3 for efficient methylation at Lys4.  This methylation is implicated in the control of activation of cell lineage genes during embryogenesis.  WDR5 interacts with histone-lysine N-methyltransferase (MLL)<ref>PMID:21531708</ref>.  <br />
*'''WD repeat-containing protein 48 and 20''' act as regulator of deubiquinating complexes.


== Disease ==
== Disease ==

Revision as of 09:36, 14 December 2016

Human WD-repeat protein 5 (grey) complex with histone H3 peptide (green) (PDB code 2h9m)

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3D Structures of WD-repeat protein 5

Updated on 14-December-2016

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman