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Structural Basis for the Product Specificity of Histone Lysine Methyltransferases

DIM-5 is a SUV39-type histone H3 Lys9 methyltransferase that is essential for DNA methylation in N. crassa. We report the structure of a ternary complex including DIM-5, S-adenosyl-l-homocysteine, and a substrate H3 peptide. The histone tail inserts as a parallel strand between two DIM-5 strands, co...

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Bibliografische gegevens
Hoofdauteurs: Zhang, Xing, Yang, Zhe, Khan, Seema I., Horton, John R., Tamaru, Hisashi, Selker, Eric U., Cheng, Xiaodong
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 2003
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2713655/
https://ncbi.nlm.nih.gov/pubmed/12887903
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