WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases
- PMID: 11814058
- PMCID: PMC11337334
- DOI: 10.1007/pl00000838
WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases
Abstract
Defined by the presence of four or more repeating units containing a conserved core of approximately 40 amino acids that usually ending with tryptophan-aspartic acid (WD), WD-repeat proteins belong to a large and fast-expanding conservative protein family. As demonstrated by the crystal structure of the G protein beta subunit, all WD-repeat proteins are speculated to form a circularized beta propeller structure. The importance of these proteins is not only demonstrated by their critical roles in many essential biological functions ranging from signal transduction, transcription regulation, to apoptosis, but is also recognized by their association with several human diseases. Defining the function of a WD-repeat protein is the current challenge. It is, however, paramount to uncover the function of individual WD-repeat proteins, explore the protein interaction mechanism through WD-repeat domains and, ultimately, understand the complex biological processes and organisms themselves.
Similar articles
-
Folding a WD repeat propeller. Role of highly conserved aspartic acid residues in the G protein beta subunit and Sec13.J Biol Chem. 1998 Apr 10;273(15):9041-9. doi: 10.1074/jbc.273.15.9041. J Biol Chem. 1998. PMID: 9535892
-
Folding of proteins with WD-repeats: comparison of six members of the WD-repeat superfamily to the G protein beta subunit.Biochemistry. 1996 Nov 5;35(44):13985-94. doi: 10.1021/bi9612879. Biochemistry. 1996. PMID: 8909296
-
Wdr12, a mouse gene encoding a novel WD-Repeat Protein with a notchless-like amino-terminal domain.Genomics. 2002 Jan;79(1):77-86. doi: 10.1006/geno.2001.6682. Genomics. 2002. PMID: 11827460
-
Phylogenetic, structural and functional relationships between WD- and Kelch-repeat proteins.Subcell Biochem. 2008;48:6-19. doi: 10.1007/978-0-387-09595-0_2. Subcell Biochem. 2008. PMID: 18925367 Review.
-
The ancient regulatory-protein family of WD-repeat proteins.Nature. 1994 Sep 22;371(6495):297-300. doi: 10.1038/371297a0. Nature. 1994. PMID: 8090199 Review.
Cited by
-
The BEACH is hot: a LYST of emerging roles for BEACH-domain containing proteins in human disease.Traffic. 2013 Jul;14(7):749-66. doi: 10.1111/tra.12069. Epub 2013 Apr 24. Traffic. 2013. PMID: 23521701 Free PMC article. Review.
-
Transcriptomics of a giant freshwater prawn (Macrobrachium rosenbergii): de novo assembly, annotation and marker discovery.PLoS One. 2011;6(12):e27938. doi: 10.1371/journal.pone.0027938. Epub 2011 Dec 8. PLoS One. 2011. PMID: 22174756 Free PMC article.
-
A compound heterozygous mutation of ERCC8 is responsible for a family with Cockayne syndrome.Mol Biol Rep. 2024 Feb 27;51(1):371. doi: 10.1007/s11033-024-09235-9. Mol Biol Rep. 2024. PMID: 38411728
-
Cellular Protein WDR11 Interacts with Specific Herpes Simplex Virus Proteins at the trans-Golgi Network To Promote Virus Replication.J Virol. 2015 Oct;89(19):9841-52. doi: 10.1128/JVI.01705-15. Epub 2015 Jul 15. J Virol. 2015. PMID: 26178983 Free PMC article.
-
Stealing the spotlight: CUL4-DDB1 ubiquitin ligase docks WD40-repeat proteins to destroy.Cell Div. 2007 Feb 6;2:5. doi: 10.1186/1747-1028-2-5. Cell Div. 2007. PMID: 17280619 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials