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Related Experiment Videos

SET domains and histone methylation.

Bing Xiao1, Jonathan R Wilson, Steven J Gamblin

  • 1Protein Structure Division, NIMR, Mill Hill, NW7 1AA London, UK.

Current Opinion in Structural Biology
|December 17, 2003
PubMed
Summary
This summary is machine-generated.

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SET domains catalyze methylation of lysine residues in chromatin regulation. Their novel structures reveal how cofactors and substrates bind, with lysine approaching methyl groups via a narrow channel.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Epigenetics

Background:

  • SET domains are crucial for chromatin regulation.
  • These domains catalyze the methylation of lysine residues.
  • Cellular, biochemical, and structural properties of SET domains are of intense interest.

Purpose of the Study:

  • To investigate the cellular, biochemical, and structural properties of SET domain proteins.
  • To understand the mechanism of lysine methylation by SET domains.

Main Methods:

  • X-ray crystallography was used to determine the structures of five SET domain proteins.
  • Biochemical assays were likely employed to study substrate binding and catalysis.

Main Results:

Related Experiment Videos

  • Five SET domain protein structures were reported.
  • SET domains exhibit a novel fold.
  • Adjacent domains contribute to structural stability and active site completion.
  • S-adenosyl-L-methionine and peptide substrates bind to opposite faces of the SET domain.
  • A narrow channel facilitates the approach of the target lysine sidechain to the methyl group.

    • Conclusions:

    • The novel structure of SET domains provides insights into their catalytic mechanism.
    • Understanding these structures aids in comprehending epigenetic regulation.
    • Further research into SET domain function and inhibition is warranted.