 |
InterPro: IPR020472 G-protein beta WD-40 repeat, region
Protein matches
|
UniProtKB Matches: 8454 proteins |
|
Accession
|
IPR020472 G-protein_beta_WD-40_rep_reg |
Type
|
Region |
Signatures
|
|
InterPro Relationships
|
|
Parent
|
IPR017986 WD40-repeat-containing domain
|
|
Found in
|
IPR016346 Guanine nucleotide-binding protein, beta subunit
IPR016391 Coatomer, alpha subunit
IPR016453 Coatomer, beta' subunit
IPR017251 Apoptotic protease-activating factor 1
IPR017252 Dynein regulator
IPR017399 WD repeat protein 23
|
|
Contains
|
IPR001680 WD40 repeat
IPR019775 WD40 repeat, conserved site
IPR019781 WD40 repeat, subgroup
|
|
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 region that spans the WD-40 repeats in members of the WD repeat G protein beta family.
|
Structural links
|
|
Additional Reading
|
|
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
|
|
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
|
|
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
|
|
Lupas AN, Lupas JM, Stock JB.
Do G protein subunits associate via a three-stranded coiled coil?
FEBS Lett. 314 1992 105-8
[PubMed: 1459238]
http://dx.doi.org/10.1016/0014-5793(92)80952-D
|
|
van der Voorn L, Ploegh HL.
The WD-40 repeat.
FEBS Lett. 307 1992 131-4
[PubMed: 1644165]
http://dx.doi.org/10.1016/0014-5793(92)80751-2
|
|
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
|
|
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
|
|
Kaziro Y, Itoh H, Kozasa T, Nakafuku M, Satoh T.
Structure and function of signal-transducing GTP-binding proteins.
Annu. Rev. Biochem. 60 1991 349-400
[PubMed: 1909108]
http://dx.doi.org/10.1146/annurev.bi.60.070191.002025
|
|
Clapham DE, Neer EJ.
New roles for G-protein beta gamma-dimers in transmembrane signalling.
Nature 365 1993 403-6
[PubMed: 8413584]
http://dx.doi.org/10.1038/365403a0
|
|
Simon MI, Strathmann MP, Gautam N.
Diversity of G proteins in signal transduction.
Science 252 1991 802-8
[PubMed: 1902986]
http://www.sciencemag.org/cgi/content/abstract/252/5007/802
|
|
Tesmer VM, Kawano T, Shankaranarayanan A, Kozasa T, Tesmer JJ.
Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex.
Science 310 2005 1686-90
[PubMed: 16339447]
http://dx.doi.org/10.1126/science.1118890
|
|
|
InterPro 24.0
|