3s8p
From Proteopedia
Contents |
Crystal Structure of the SET Domain of Human Histone-Lysine N-Methyltransferase SUV420H1 In Complex With S-Adenosyl-L-Methionine
Template:ABSTRACT PUBMED 24396869
Function
[SV421_HUMAN] Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity).
About this Structure
3s8p is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA.
See Also
Reference
- Wu H, Siarheyeva A, Zeng H, Lam R, Dong A, Wu XH, Li Y, Schapira M, Vedadi M, Min J. Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2. FEBS Lett. 2013 Nov 29;587(23):3859-68. PMID:24396869
Categories: Histone-lysine N-methyltransferase | Human | Arrowsmith, C H. | Bountra, C. | Edwards, A M. | Lam, R. | Loppnau, P. | Min, J. | SGC, Structural Genomics Consortium. | Weigelt, J. | Wu, H. | Zeng, H. | Chromosome | Histone lysine | Histone methyltransferase | Methylation | Nucleus | Sam | Set domain | Sgc | Structural genomic | Structural genomics consortium | Transcription regulation | Transferase