 |
InterPro: IPR019782 WD40 repeat 2
Protein matches
|
UniProtKB Matches: 21107 proteins |
|
Accession
|
IPR019782 WD40_repeat_2 |
Type
|
Repeat |
Signatures
|
|
InterPro Relationships
|
|
Parent
|
IPR019781 WD40 repeat, subgroup
|
|
Found in
|
IPR000664 Lethal(2) giant larvae protein
IPR001632 G-protein, beta subunit
IPR009146 Groucho/transducin-like enhancer
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
IPR016453 Coatomer, beta' subunit
IPR017149 Glutathione degradosome, DUG2
IPR017233 WD repeat protein 35
IPR017251 Apoptotic protease-activating factor 1
IPR017252 Dynein regulator
IPR017383 Actin-related protein 2/3 complex, subunit 1
IPR017399 WD repeat protein 23
IPR017422 WD repeat protein 55
IPR017986 WD40-repeat-containing domain
|
|
Contains
|
IPR019775 WD40 repeat, conserved site
|
|
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. The repeat profile in this entry represents the central core of the domain (positions 9 to 23).
|
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
|
|
Nolen BJ, Pollard TD.
Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex.
Mol. Cell 26 2007 449-57
[PubMed: 17499050]
http://dx.doi.org/10.1016/j.molcel.2007.04.017
|
|
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
|
|
Larsen NA, Al-Bassam J, Wei RR, Harrison SC.
Structural analysis of Bub3 interactions in the mitotic spindle checkpoint.
Proc. Natl. Acad. Sci. U.S.A. 104 2007 1201-6
[PubMed: 17227844]
http://dx.doi.org/10.1073/pnas.0610358104
|
|
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
|
|
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
|