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3pnw
From Proteopedia
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| - | [[Image:3pnw.png|left|200px]] | ||
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{{STRUCTURE_3pnw| PDB=3pnw | SCENE= }} | {{STRUCTURE_3pnw| PDB=3pnw | SCENE= }} | ||
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===Crystal Structure of the tudor domain of human TDRD3 in complex with an anti-TDRD3 FAB=== | ===Crystal Structure of the tudor domain of human TDRD3 in complex with an anti-TDRD3 FAB=== | ||
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{{ABSTRACT_PUBMED_23219464}} | {{ABSTRACT_PUBMED_23219464}} | ||
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| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/TDRD3_HUMAN 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.<ref>PMID:18632687</ref> <ref>PMID:15955813</ref> <ref>PMID:21172665</ref> | ||
==About this Structure== | ==About this Structure== | ||
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==See Also== | ==See Also== | ||
*[[Antibody|Antibody]] | *[[Antibody|Antibody]] | ||
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:023219464</ref><references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
Revision as of 02:51, 20 September 2013
Contents |
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
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
- ↑ 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
- ↑ 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
- ↑ 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
Categories: Homo sapiens | Synthetic construct | Adams-Cioaba, M A. | Arrowsmith, C H. | Bountra, C. | Cossar, D. | Edwards, A M. | Lam, R. | Loppnau, P. | Persson, H. | Ravichandran, M. | SGC, Structural Genomics Consortium. | Sidhu, S S. | Tempel, W. | Weigelt, J. | Wernimont, A K. | Antibody | Fab | Protein binding-immune system complex | Sgc | Structural genomics consortium
