 |
InterPro: IPR019775 WD40 repeat, conserved site
Protein matches
|
UniProtKB Matches: 14615 proteins |
|
Accession
|
IPR019775 WD40_repeat_CS |
Type
|
Conserved_site |
Signatures
|
|
InterPro Relationships
|
|
Found in
|
IPR000009 Protein phosphatase 2A, regulatory subunit PR55
IPR000664 Lethal(2) giant larvae protein
IPR001632 G-protein, beta subunit
IPR001680 WD40 repeat
IPR011046 WD40 repeat-like-containing domain
IPR015505 Coronin
IPR015943 WD40/YVTN repeat-like-containing domain
IPR016346 Guanine nucleotide-binding protein, beta subunit
IPR016391 Coatomer, alpha subunit
IPR017149 Glutathione degradosome, DUG2
IPR017251 Apoptotic protease-activating factor 1
IPR017252 Dynein regulator
IPR017422 WD repeat protein 55
IPR017986 WD40-repeat-containing domain
IPR019578 Serine-threonine phosphatase 2A, subunit B, alpha/ beta central domain
IPR019781 WD40 repeat, subgroup
IPR019782 WD40 repeat 2
IPR020472 G-protein beta WD-40 repeat, region
|
|
InterPro annotation
|
|
Entry Details in BioMart
|
Abstract
|
WD-40 repeats (also known as WD or beta-transducin repeats) are short ~40 amino acid motifs, often terminating in a Trp-Asp (W-D) dipeptide. WD40 repeats usually assume a 7-8 bladed beta-propeller fold, but proteins have been found with 4 to 16 repeated units, which also form a circularised beta-propeller structure. WD-repeat proteins are a large family found in all eukaryotes and are implicated in a variety of functions ranging from signal transduction and transcription regulation to cell cycle control and apoptosis. Repeated WD40 motifs act as a site for protein-protein interaction, and proteins containing WD40 repeats are known to serve as platforms for the assembly of protein complexes or mediators of transient interplay among other proteins. The specificity of the proteins is determined by the sequences outside the repeats themselves. Examples of such complexes are G proteins (beta subunit is a beta-propeller), TAFII transcription factor, and E3 ubiquitin ligase [1, 2]. In Arabidopsis spp., several WD40-containing proteins act as key regulators of plant-specific developmental events. This entry represents a conserved site found in the WD40 repeat.
|
Structural links
|
|
Additional Reading
|
|
Hao B, Oehlmann S, Sowa ME, Harper JW, Pavletich NP.
Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases.
Mol. Cell 26 2007 131-43
[PubMed: 17434132]
http://dx.doi.org/10.1016/j.molcel.2007.02.022
|
|
Gilman AG.
G proteins: transducers of receptor-generated signals.
Annu. Rev. Biochem. 56 1987 615-49
[PubMed: 3113327]
http://dx.doi.org/10.1146/annurev.bi.56.070187.003151
|
|
Davis TL, Bonacci TM, Sprang SR, Smrcka AV.
Structural and molecular characterization of a preferred protein interaction surface on G protein beta gamma subunits.
Biochemistry 44 2005 10593-604
[PubMed: 16060668]
http://dx.doi.org/10.1021/bi050655i
|
|
Duronio RJ, Gordon JI, Boguski MS.
Comparative analysis of the beta transducin family with identification of several new members including PWP1, a nonessential gene of Saccharomyces cerevisiae that is divergently transcribed from NMT1.
Proteins 13 1992 41-56
[PubMed: 1594577]
http://dx.doi.org/10.1002/prot.340130105
|
|
Johnston CA, Kimple AJ, Giguere PM, Siderovski DP.
Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gbeta1gamma2.
Structure 16 2008 1086-94
[PubMed: 18611381]
http://dx.doi.org/10.1016/j.str.2008.04.010
|
|
Cheever ML, Snyder JT, Gershburg S, Siderovski DP, Harden TK, Sondek J.
Crystal structure of the multifunctional Gbeta5-RGS9 complex.
Nat. Struct. Mol. Biol. 15 2008 155-62
[PubMed: 18204463]
http://dx.doi.org/10.1038/nsmb.1377
|
|
Jennings BH, Pickles LM, Wainwright SM, Roe SM, Pearl LH, Ish-Horowicz D.
Molecular recognition of transcriptional repressor motifs by the WD domain of the Groucho/TLE corepressor.
Mol. Cell 22 2006 645-55
[PubMed: 16762837]
http://dx.doi.org/10.1016/j.molcel.2006.04.024
|
|
Neer EJ, Schmidt CJ, Nambudripad R, Smith TF.
The ancient regulatory-protein family of WD-repeat proteins.
Nature 371 1994 297-300
[PubMed: 8090199]
http://dx.doi.org/10.1038/371297a0
|
|
|
InterPro 23.1
|