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InterPro: IPR020472 G-protein beta WD-40 repeat, region

Protein matchesHelp
UniProtKB
Matches:
8454 proteins
AccessionHelp IPR020472 G-protein_beta_WD-40_rep_reg
TypeHelp Region
SignaturesHelp
InterPro RelationshipsHelp
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
BioMart Logo Entry Details in BioMart
AbstractHelp

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 linksHelp
SCOP: b.69.4.1
CATH: 2.130.10.10

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR020472 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O14727 Apoptotic protease-activating factor 1

P07834 Cell division control protein 4

P62881 Guanine nucleotide-binding protein subunit beta-5

Q11176 Actin-interacting protein 1

Q24572 Probable histone-binding protein Caf1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002182 NB-ARC
IPR019775 WD40 repeat, conserved site
IPR017986 WD40-repeat-containing domain
IPR019782 WD40 repeat 2
IPR001810 Cyclin-like F-box
IPR019781 WD40 repeat, subgroup
IPR011029 DEATH-like
IPR001632 G-protein, beta subunit
IPR017251 Apoptotic protease-activating factor 1
IPR011046 WD40 repeat-like-containing domain
IPR001680 WD40 repeat
IPR001315 Caspase Recruitment
IPR016346 Guanine nucleotide-binding protein, beta subunit
IPR020472 G-protein beta WD-40 repeat, region
IPR000767 Disease resistance protein
IPR015943 WD40/YVTN repeat-like-containing domain
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Li D, Roberts R.
WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases.
Cell. Mol. Life Sci. 58 2085-97 2001 [PubMed: 11814058]
http://dx.doi.org/10.1007/PL00000838
2. Smith TF, Gaitatzes C, Saxena K, Neer EJ.
The WD repeat: a common architecture for diverse functions.
Trends Biochem. Sci. 24 181-5 1999 [PubMed: 10322433]
http://dx.doi.org/10.1016/S0968-0004(99)01384-5

Additional ReadingHelp
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
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InterPro 24.0