3dlm
From Proteopedia
Crystal structure of Tudor domain of human Histone-lysine N-methyltransferase SETDB1
Structural highlights
FunctionSETB1_HUMAN Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.[1] [2] [3] [4] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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Categories: Homo sapiens | Large Structures | Amaya MF | Arrowsmith CH | Bochkarev A | Bountra C | Dombrovski L | Edwards AM | Loppnau P | Min J | Weigelt J | Wu H