Tudor domains

Huang Y, Fang J, Bedford MX, Zhang Y, Xu RM (2006) Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312 748—751 Ichimura T, Watanabe S, Sakamoto Y, Aoto T, Fujita N, Nakao M (2005) Transcriptional repression and heterochromatin formation by MBDl and MCAF/AM family proteins. J Biol Chem 280(14) 13928-13935... 

Maurer-Stroh, S., Dickens, N.J., Hughes-Davies, L., Kouzarides, T., Eisenhaber, F. and Ponting, C.P. (2003) The Tudor domain Royal Family Tudor, plant Agenet, Chromo, PWWP and MBT domains. Trends in Biochemical Sciences, 28, 69-74. 

Zhang, Y. and Xu, R.M. (2006) Recognition ofhistone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science, 312, 748-751. 

Cote, J. and Richard, S. (2005) Tudor domains bind symmetrical dimethylated arginines. The Journal of Biological Chemistry, 280, 28476-28483. 

Huyen Y, et al. Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks. Nature 2004 432 406 11. Flanagan JF, et al. Double chromodomains cooperate to recognize the methylated histone H3 tail. Nature 2005 438 1181-1185. Cote J, Richard S. Tudor domains bind symmetrical dimethylated arginines. J. Biol. Chem. 2005 280 28476-28483. 

Sprangers R, Groves MR, Sinning I, Sattler M. High-resolution X-ray and NMR strucmres of the SMN tudor domain conformational variation in the binding site for symmetrically dimethylated arginine residues. J. Mol. Biol. 2003 327 507-520. 

Histone acetyl transferases (HATs, EC 2.3.1.48 Table 5.1) catalyse the transfer of an acetyl group to the s-amino group of lysine residues in the tails and/or cores of histones, although, as for HDACs, some HATs also modify non-his-tone substrates e.g. transcription factors). HATs generally contain multiple subunits, and the functions of the catalytic subunit depend on the presence of other subunits. Domains that cooperate to recruit the HAT to the appropriate location in the genome include bromodomains, chromodomains, WD40 repeats, Tudor domains and PHD fingers. ... 

Tandem Tudor domain (JMJD2A) 2GFA Surface recognition Kme3 preference 3 aromatic + 1 acidic... 

Similarly, Grzesiek and co-workers " have compared Dhn RDCs measured in solution with those calculated from the crystal structure to characterize conformations of ABL kinase in a complex with three clinical inhibitors Jasco et al have investigated structural differences of MalF-P2 in solution and in the crystalline state Sattler and co-workers have compared solution and crystal structures of the extended Tudor domain of D. melanogasler Tudor-SN Zweckstetter and co-workers have compared RDCs calculated for X-Ray and model structures of CesT with those measured in solution to point that this protein exists in solution as the unswapped dimer. In a similar manner Clore and co-workers have studied the impact of phosphorylation on structure and interactions between N-terminal domain of enzyme I (EIN) and the histidine phospho-carrier protein (HPr). Table 6 provides several examples of proteins whose structures were solved or refined using RDCs. 

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