2003
DOI: 10.1016/s0022-2836(03)00148-7
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High-resolution X-ray and NMR Structures of the SMN Tudor Domain: Conformational Variation in the Binding Site for Symmetrically Dimethylated Arginine Residues

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Cited by 162 publications
(142 citation statements)
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“…The MBT repeat consists of a five-stranded ␤-barrel core domain that shares struc-tural similarity to the Tudor and chromodomains. The Tudor domain interacts with methylated arginine residues (Sprangers et al 2003), and chromodomains interact with methylated lysine residues of histone H3 (Bannister et al 2001;Lachner et al 2001;Nakayama et al 2001;Cao et al 2002). Consistent with the speculation that this domain is critical for function of the MBT family and that the proteins bind modified histones, several hypomorphic mutations in Drosophila SCM map to residues within in the putative ligand-binding pocket (Bornemann et al 1998;Wang et al 2003).…”
Section: A Conserved Complex For Repressionmentioning
confidence: 86%
“…The MBT repeat consists of a five-stranded ␤-barrel core domain that shares struc-tural similarity to the Tudor and chromodomains. The Tudor domain interacts with methylated arginine residues (Sprangers et al 2003), and chromodomains interact with methylated lysine residues of histone H3 (Bannister et al 2001;Lachner et al 2001;Nakayama et al 2001;Cao et al 2002). Consistent with the speculation that this domain is critical for function of the MBT family and that the proteins bind modified histones, several hypomorphic mutations in Drosophila SCM map to residues within in the putative ligand-binding pocket (Bornemann et al 1998;Wang et al 2003).…”
Section: A Conserved Complex For Repressionmentioning
confidence: 86%
“…Disruption of these domains mislocalizes the chromatin association of each protein and has distinct functional consequences. One tudor domain was originally shown to bind a methylated arginine residue, 89 and so the histone primary sequence, composition, or context may be the determining factor between lysine and arginine binding. In addition to the chromo-and tudor domain families, the PWWP, MBT, and Agenet family members show sequence and structure similarity to proteins known to associate with methylated peptides and have all been grouped into the tudor domain 'Royal Family' of proteins.…”
Section: Other Histone Methylation Sites and Methyl Lysine/ Arginine mentioning
confidence: 99%
“…Fig. 2D shows the Tudor domain structure of survival motor neuron (SMN), the spinal muscular atrophy protein (36). The Sir1p C-terminal lobe superimposes well with the SMN Tudor domain.…”
Section: Resultsmentioning
confidence: 99%