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PROSITE documentation PDOC51641 [for PROSITE entry PS51641]

Agenet-like domain profile





Description

Fragile X Mental Retardation Protein (FMRP), and its autosomal paralogues, Fragile X mental Retardation syndrome-related protein 1 and 2 (FXR1 and FXR2), comprise a family of RNA-binding proteins. It is thought that the FRMP family of proteins contributes to the regulation of protein synthesis at sites where mRNAs are locally translated in response to stimuli. These proteins are highly similar to one another and also retain highly conserved domain architecture. The two ribonucleoprotein K homology (KH) domains (see <PDOC50084>) and the cluster of arginine and glycine residues that constitute the RGG box, comprise a large region that is important for RNA binding and polyribosome association. In addition, two Agenet-like domains exist in tandem within the N-terminal regions of FMRP family proteins. The Agenet-like domain belongs to the "Royal" domain superfamilly which contains also the Tudor (see <PDOC50304>), chromo (see <PDOC00517>), MBT (see <PDOC51079>), PWWP (see <PDOC50812>) and plant Agenet domains. Biochemical analysis of the tandem Agenet-like domains reveals their ability to preferentially recognize trimethylated peptides in a sequence-specific manner [1,2,3,4].

The Agenet-like domain folds into a bent four-stranded antiparallel β sheet with a fifth strand closing the cavity of the sheet, similar to a thumb accross a semiclosed hand (see <PDB:2BKD>) [3,4].

The profile we developed covers the entire Agenet-like domain.

Last update:

March 2012 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

AGENET_LIKE, PS51641; Agenet-like domain profile  (MATRIX)


References

1AuthorsMaurer-Stroh S. Dickens N.J. Hughes-Davies L. Kouzarides T. Eisenhaber F. Ponting C.P.
TitleThe Tudor domain 'Royal Family': Tudor, plant Agenet, Chromo, PWWP and MBT domains.
SourceTrends Biochem. Sci. 28:69-74(2003).
PubMed ID12575993

2AuthorsAdinolfi S. Ramos A. Martin S.R. Dal Piaz F. Pucci P. Bardoni B. Mandel J.L. Pastore A.
TitleThe N-terminus of the fragile X mental retardation protein contains a novel domain involved in dimerization and RNA binding.
SourceBiochemistry 42:10437-10444(2003).
PubMed ID12950170
DOI10.1021/bi034909g

3AuthorsRamos A. Hollingworth D. Adinolfi S. Castets M. Kelly G. Frenkiel T.A. Bardoni B. Pastore A.
TitleThe structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction.
SourceStructure 14:21-31(2006).
PubMed ID16407062
DOI10.1016/j.str.2005.09.018

4AuthorsAdams-Cioaba M.A. Guo Y. Bian C. Amaya M.F. Lam R. Wasney G.A. Vedadi M. Xu C. Min J.
TitleStructural studies of the tandem Tudor domains of fragile X mental retardation related proteins FXR1 and FXR2.
SourcePLoS ONE 5:E13559-E13559(2010).
PubMed ID21072162
DOI10.1371/journal.pone.0013559



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