3omc
From Proteopedia
Contents |
Structure of human SND1 extended tudor domain in complex with the symmetrically dimethylated arginine PIWIL1 peptide R4me2s
Template:ABSTRACT PUBMED 20937909
Function
[SND1_HUMAN] Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2).[1]
About this Structure
3omc is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Liu K, Chen C, Guo Y, Lam R, Bian C, Xu C, Zhao DY, Jin J, MacKenzie F, Pawson T, Min J. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18398-403. Epub 2010 Oct 11. PMID:20937909 doi:10.1073/pnas.1013106107
- ↑ Tong X, Drapkin R, Yalamanchili R, Mosialos G, Kieff E. The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE. Mol Cell Biol. 1995 Sep;15(9):4735-44. PMID:7651391
Categories: Homo sapiens | Arrowsmith, C H. | Bian, C B. | Bochkarev, A. | Bountra, C. | Edwards, A M. | Guo, Y H. | Lam, R. | Liu, K. | MacKenzie, F. | Min, J. | SGC, Structural Genomics Consortium. | Weigelt, J. | Xu, C. | P100 extended tudor domain | Piwil1/miwi | Sgc | Snd1 | Staphylococcal nuclease domain-containing protein 1 | Structural genomics consortium | Symmetrically dimethylated arginine peptides derived from piwil1 | Tdrd11 | Transcription regulation | Transcription regulator