WD40 repeat: Difference between revisions

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1b9x, 1b9y, 1erj, 1gg2, 1got, 1gp2, 1gxr, 1nex, 1nr0, 1omw, 1p22, 1pev, 1pgu, 1pi6, 1s4u, 1sq9, 1tbg, 1u4c, 1xhm, 1yfq, 2bcj, 2ce8, 2ce9, 2trc

WD domain, G-beta repeat
WD domain, G-beta repeat
Identifiers
Symbol	WD40
Pfam	PF00400
InterPro	IPR001680
PROSITE	PDOC00574
SCOP2	1gp2 / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1b9x, 1b9y, 1erj, 1gg2, 1got, 1gp2, 1gxr, 1nex, 1nr0, 1omw, 1p22, 1pev, 1pgu, 1pi6, 1s4u, 1sq9, 1tbg, 1u4c, 1xhm, 1yfq, 2bcj, 2ce8, 2ce9, 2trc

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Revision as of 19:31, 28 January 2009

The WD40 repeat (also known as the WD or beta-transducin repeat) is a short ~40 amino acid motif, often terminating in a tryptophan-aspartic acid (W-D) dipeptide.^[1] Several of these repeats are combined to form a type of protein domain called the WD domain.

Structure

WD-containing proteins have 4 to 16 repeating units, all of which are thought to form a circularised beta-propeller structure.^[2]^[3]

Function

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. The underlying common function of all WD-repeat proteins is coordinating multi-protein complex assemblies, where the repeating units serve as a rigid scaffold for protein interactions. 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.^[2]^[3]

References

^ Neer EJ, Schmidt CJ, Nambudripad R, Smith TF (1994). "The ancient regulatory-protein family of WD-repeat proteins". Nature. 371 (6495): 297–300. doi:10.1038/371297a0. PMID 8090199. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
^ ^a ^b Smith TF, Gaitatzes C, Saxena K, Neer EJ (1999). "The WD repeat: a common architecture for diverse functions". Trends Biochem. Sci. 24 (5): 181–5. doi:10.1016/S0968-0004(99)01384-5. PMID 10322433. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
^ ^a ^b Li D, Roberts R (2001). "WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases". Cell. Mol. Life Sci. 58 (14): 2085–97. doi:10.1007/PL00000838. PMID 11814058. {{cite journal}}: Unknown parameter |month= ignored (help)

This article incorporates text from the public domain Pfam and InterPro: IPR001680

[pmid8090199-1] Neer EJ, Schmidt CJ, Nambudripad R, Smith TF (1994). "The ancient regulatory-protein family of WD-repeat proteins". Nature. 371 (6495): 297–300. doi:10.1038/371297a0. PMID 8090199. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)

[pmid10322433-2] Smith TF, Gaitatzes C, Saxena K, Neer EJ (1999). "The WD repeat: a common architecture for diverse functions". Trends Biochem. Sci. 24 (5): 181–5. doi:10.1016/S0968-0004(99)01384-5. PMID 10322433. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)

[pmid11814058-3] Li D, Roberts R (2001). "WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases". Cell. Mol. Life Sci. 58 (14): 2085–97. doi:10.1007/PL00000838. PMID 11814058. {{cite journal}}: Unknown parameter |month= ignored (help)

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