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WD repeat-containing protein: Difference between revisions

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<StructureSection load='' size='340' side='right' caption='Human WD-repeat protein 5 (deepskyblue) complex with histone H3 peptide (magenta) (PDB code [[2h9m]])' scene='70/709459/Cv/1'>
<StructureSection load='' size='340' side='right' caption='Human WD-repeat protein 5 (deepskyblue) complex with histone H3 peptide (magenta) (PDB code [[2h9m]])' scene='70/709459/Cv/1'>
== Function ==
== Function ==
'''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-containing proteins''' or '''ribosome biogenesis protein WDR''' (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 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 regulators of deubiquinating complexes.
*'''WD repeat-containing protein 48 and 20''' act as regulators of deubiquinating complexes.


*'''WD repeat-containing protein 41''' is the non-catalytic component of C9orf72-SMCR8 complex which regulates autophagy<ref>PMID:27193190</ref>.  <br />
*'''WD repeat-containing protein 55''' is a modulator of rRNA synthesis.  <br />
*'''WD repeat-containing protein 61''' is a component of PAF1 complex which functions during RNA transcription.  <br />
*'''WD repeat-containing protein 91''' functions as negative regulator of the PI3 kinase/PI3K activity in endosomal transport<ref>PMID:27126989</ref>.  <br />
*'''WD repeat-containing protein 92''' is a modulator of apoptosis.  <br />
*'''WD repeat-containing protein SLP1''' is required for mad2-dependent spindle checkpoint activation.  <br />
*'''WD repeat protein CSA''' or '''DNA excision repair protein ERCC-8''' is part of the transcription-coupled repair complex<ref>PMID:32355176</ref>.  <br />
== Disease ==
== Disease ==
Mutant WDR is involved in triple-A syndrome<ref>PMID:11062474</ref>.
Mutant WDR is involved in triple-A syndrome<ref>PMID:11062474</ref>.
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== Structural highlights ==
== Structural highlights ==
The <scene name='70/709459/Cv/4'>histone Arg2 residue inserts into the central pore</scene> of the WDR5 β-propellor structure acting like an anchoring pin <scene name='70/709459/Cv/3'>forming numerous hydrogen bonds and cation-π interactions</scene><ref>PMID:16946699</ref>. Water molecules are shown as red spheres.
The <scene name='70/709459/Cv/4'>histone Arg2 residue inserts into the central pore</scene> of the WDR5 β-propellor structure acting like an anchoring pin <scene name='70/709459/Cv/3'>forming numerous hydrogen bonds and cation-π interactions</scene><ref>PMID:16946699</ref>. Water molecules are shown as red spheres.
 
== 3D Structures of WD-repeat protein ==
[[WD-repeat protein 3D structures]]
</StructureSection>
</StructureSection>


== 3D Structures of WD-repeat protein ==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*WDR5
**[[2gnq]], [[2h68]], [[2h14]], [[2h9l]] – hWDR5 – human<br />
**[[3mxx]], [[3n0d]], [[3n0e]] – hWDR5 (mutant)<br />
**[[3smr]], [[3ur4]], [[4ia9]], [[4qqe]], [[4ql1]], [[5eal]], [[5eam]], [[5eap]], [[5ear]] – hWDR5 + piperazine derivative<br />
**[[2cnx]], [[2co0]], [[2h6k]], [[2h6n]], [[2h6q]], [[2h13]], [[2h9m]], [[2h9n]], [[2h9p]], [[2g99]], [[2g9a]], [[2o9k]], [[3psl]], [[4a7j]] – hWDR5 + histone H3 peptide<br />
**[[5vfc]], [[6dar]], [[6das]], [[6d9x]], [[6dai]], [[6dak]] – hWDR5 + inhibitor<br />
**[[4gm3]], [[4gm8]], [[4gm9]], [[4gmb]] – hWDR5 + peptide inhibitor<br />
**[[2xl2]], [[2xl3]] – hWDR5 + retinoblastoma-binding protein 5 peptide<br />
**[[4o45]] – hWDR5 + influenza NS1 C-terminal<br />
**[[4cy1]] – hWDR5 + KAT8 regulatory NSL complex subunit 1+2 peptides<br />
**[[4cy2]] – hWDR5 + KAT8 regulatory NSL complex subunit 1 peptide<br />
**[[4y7r]] – hWDR5 + Myc MbIIIb peptide<br />
**[[3eg6]], [[3emh]], [[3uvk]], [[3uvl]], [[3uvm]], [[3uvn]], [[3uvo]], [[4erq]], [[4ery]], [[4es0]], [[4esg]], [[4ewr]], [[5sxm]] – hWDR5 + MLL peptide<br />
**[[4erz]] – hWDR5 + MLL4<br />
**[[6byn]] – hWDR5 + monobody<br />
**[[3p4f]] – hWDR5 + retinoblastoma-binding protein 5 peptide + MLL peptide<br />
*WDR9
**[[2q2e]] – hWDR9 residues 1310-1430<br />
*WDR20
**[[5k19]] – hWDR20<br />
*WDR48
**[[5cvl]] – hWDR48 <br />
**[[5l8e]] – hWDR48 + peptide<br />
**[[5l8w]], [[5cvn]], [[5cvo]] – hWDR48 + ubiquitin + ubiquitin carboxyl-terminal hydrolase<br />
**[[5k1a]], [[5k1b]] – hWDR48 + ubiquitin carboxyl-terminal hydrolase<br />
**[[5k1c]] – hWDR48 + WDR20 + ubiquitin carboxyl-terminal hydrolase<br />
*WDR61
**[[3ow8]] – hWDR61<br />
*WDR92
**[[2q2e]] – hWDR92<br />
*WDR SLP1
**[[4aez]] – WDR + mitotic spindle checkpoint component mad2-mad3 - fission yeast <br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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