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Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3

Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3

Kenneth W Foreman, Mark Brown, Frances Park, Spencer Emtage, June Harriss, Chhaya Das, Li Zhu, Andy Crew, Lee Arnold, Salam Shaaban, Philip Tucker

PLoS One. 2011;6(7):e22290.

PMID: 21779408

Abstract:

The SET and MYND Domain (SMYD) proteins comprise a unique family of multi-domain SET histone methyltransferases that are implicated in human cancer progression. Here we report an analysis of the crystal structure of the full length human SMYD3 in a complex with an analog of the S-adenosyl methionine (SAM) methyl donor cofactor. The structure revealed an overall compact architecture in which the "split-SET" domain adopts a canonical SET domain fold and closely assembles with a Zn-binding MYND domain and a C-terminal superhelical 9 α-helical bundle similar to that observed for the mouse SMYD1 structure. Together, these structurally interlocked domains impose a highly confined binding pocket for histone substrates, suggesting a regulated mechanism for its enzymatic activity. Our mutational and biochemical analyses confirm regulatory roles of the unique structural elements both inside and outside the core SET domain and establish a previously undetected preference for trimethylation of H4K20.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42413449	Histone H4 full length human			Price

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