3pnw

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Template:STRUCTURE 3pnw

Contents 1 Crystal Structure of the tudor domain of human TDRD3 in complex with an anti-TDRD3 FAB 2 Function 3 About this Structure 4 See Also 5 Reference

Crystal Structure of the tudor domain of human TDRD3 in complex with an anti-TDRD3 FAB

Template:ABSTRACT PUBMED 23219464

Function

[TDRD3_HUMAN] Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In nucleus, acts as a coactivator: recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In cytoplasm, may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins.^{[1] [2] [3]}

About this Structure

3pnw is a 24 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA.

See Also

• Antibody

Reference

• Persson H, Ye W, Wernimont A, Adams JJ, Lam R, Sidhu SS. CDR-H3 Diversity Is Not Required for Antigen Recognition by Synthetic Antibodies. J Mol Biol. 2012 Dec 3. pii: S0022-2836(12)00909-6. doi:, 10.1016/j.jmb.2012.11.037. PMID:23219464 doi:10.1016/j.jmb.2012.11.037

1. ↑ Goulet I, Boisvenue S, Mokas S, Mazroui R, Cote J. TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules. Hum Mol Genet. 2008 Oct 1;17(19):3055-74. doi: 10.1093/hmg/ddn203. Epub 2008 Jul , 15. PMID:18632687 doi:10.1093/hmg/ddn203
2. ↑ Cote J, Richard S. Tudor domains bind symmetrical dimethylated arginines. J Biol Chem. 2005 Aug 5;280(31):28476-83. Epub 2005 Jun 6. PMID:15955813 doi:M414328200
3. ↑ Yang Y, Lu Y, Espejo A, Wu J, Xu W, Liang S, Bedford MT. TDRD3 is an effector molecule for arginine-methylated histone marks. Mol Cell. 2010 Dec 22;40(6):1016-23. doi: 10.1016/j.molcel.2010.11.024. PMID:21172665 doi:10.1016/j.molcel.2010.11.024