ArticlePloS one2012
Identifying the hotspots on the top faces of WD40-repeat proteins from their primary sequences by β-bulges and DHSW tetrads.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- High-variance phenome database reveals important roles of WD40 proteins in the plant pathogenic fungus Fusarium graminearum.The New phytologist · 2026Article
- Promiscuous RNA binding by WDR5 remodels the KMT2A (MLL1) histone methyltransferase complex to an inactive state.Molecular cell · 2026Article
- Promiscuous RNA binding by WDR5 remodels the KMT2A (MLL1) histone methyltransferase complex to an inactive state.bioRxiv : the preprint server for biology · 2026Article
- Two cases of TBL1XR1 heterozygous variants in children: a new splicing site variant identification and functional analysis through molecular docking and molecular dynamics simulation.Human genomics · 2025Article
- DCAF7 recruits USP2 to facilitate hepatocellular carcinoma progression by suppressing clockophagy-induced ferroptosis.Cell death & disease · 2025Article
- A VPS13D spastic ataxia mutation disrupts the conserved adaptor-binding site in yeast Vps13.Human molecular genetics · 2020Article
- PcG Proteins MSI1 and BMI1 Function Upstream of miR156 to Regulate Aerial Tuber Formation in Potato.Plant physiology · 2020Article
- Genome Wide Analysis of WD40 Proteins in Saccharomyces cerevisiae and Their Orthologs in Candida albicans.The protein journal · 2019Article
- The Cajal Body Protein WRAP53β Prepares the Scene for Repair of DNA Double-Strand Breaks by Regulating Local Ubiquitination.Frontiers in molecular biosciences · 2019Review
- RAMOSA1 ENHANCER LOCUS2-Mediated Transcriptional Repression Regulates Vegetative and Reproductive Architecture.Plant physiology · 2019Article
- Ciliary proteins Fap43 and Fap44 interact with each other and are essential for proper cilia and flagella beating.Cellular and molecular life sciences : CMLS · 2018Article
- PPI network analyses of human WD40 protein family systematically reveal their tendency to assemble complexes and facilitate the complex predictions.BMC systems biology · 2018Article
- The WD40 domain of ATG16L1 is required for its non-canonical role in lipidation of LC3 at single membranes.The EMBO journal · 2018Article
- Prokaryotic and Highly-Repetitive WD40 Proteins: A Systematic Study.Scientific reports · 2017Article
- Missense mutations in the WD40 domain ofJournal of medical genetics · 2017Article
- Remarkable Evolutionary Conservation of Antiobesity ADIPOSE/WDTC1 Homologs in Animals and Plants.Genetics · 2017Article
- Structure of the MeCP2-TBLR1 complex reveals a molecular basis for Rett syndrome and related disorders.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Planar Cell Polarity Effector Fritz Interacts with Dishevelled and Has Multiple Functions in Regulating PCP.G3 (Bethesda, Md.) · 2017Article
- Recurrent somatic mutations in POLR2A define a distinct subset of meningiomas.Nature genetics · 2016Article
- A WDR Gene Is a Conserved Member of a Chitin Synthase Gene Cluster and Influences the Cell Wall in Aspergillus nidulans.International journal of molecular sciences · 2016Article
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5 authors.
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Abstract
The analysis of 36 available crystal structures of WD40 repeat proteins reveals widespread existence of a beta-bulge formed at the beginning of strand a and the end of strand b, termed as WD(b-a) bulge: among a total of 259 WD40 blades, there are 243 such β-bulges. The R(1) positions in these WD(b-a) bulges have fair distributions of Arg, His, Ile, Leu, Lys, Met, Phe, Trp, Tyr and Val residues. These residues protrude on the top face of the WD40 proteins and can serve as hotspots for protein-protein interactions. An analysis of 29 protein complexes formed by 17 WD proteins reveals that these R(1) residues, along with two other residues (R(1)-2 and D-1), are indeed widely involved in protein-protein interactions. Interestingly, these WD(b-a) bulges can be easily identified by the 4-amino acid sequences of (V, L, I), R(1), R(2), (V, L, I), along with some other significant amino acids. Thus, the hotspots of WD40 proteins on the top face can be readily predicted based on the primary sequences of the proteins. The literature-reported mutagenesis studies for Met30, MDV1, Tup11, COP1 and SPA1, which crystal structures are not available, can be readily understood based on the feature-based method. Applying the method, the twelve potential hotspots on the top face of Tup11 from S. japonicas have been identified. Our ITC measurements confirm seven of them, Tyr382, Arg284, Tyr426, Tyr508, Leu559, Lys575 and Ile601, are essential for recognizing Fep1. The ITC measurements further convinced that the feature-based method provides accurate prediction of hotspots on the top face.
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