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CHROMO Domain
Structure:

No Image The Chromo domain appears as an N-terminal three-stranded anti-parallel b-sheet which folds against an N-terminal a-helix. A conserved series of hydrophobic residues that winds across the face of the b-sheet is referred to as a sash. Interactions with partner proteins are thought to be mediated by the residues within the hydrophobic sash. The figure shows the structure of the chromo domain from mouse modifier protein 1.

Structure Reference:
Jacobs, SA. et al. (2002) Science. 295(5562): 2080-3. PDB: 1KNA.

Domain binding and function:
The Chromatin Organization Modifier (Chromo) domain is defined as a 3070 amino acid residue protein module found in a number of proteins involved in the assembly of protein complexes on chromatin. This domain was first described in Drosophila modifiers of variegation proteins that modify the structure of chromatin to the condensed morphology of heterochromatin, a cytologically visible region within which gene expression is repressed. Examples of chromo-domain-containing proteins include the HP1 the Polycomb (Pc) transcriptional repressors and the human retinoblastoma binding protein (RBP-1). Chromo domains function to promote binding to methylated lysines in the tail region of Histone H3.   Chromo domains can function individually or in tandem such as CHD1 to recognize specific methylated Histone tails.
Examples of Proteins: 
CROMO domain protein
Binding partner
HP1 Histone H3 methylated lysine-9
Polycomb Proteins

Histone H3 methylated lysine-27
CHD1

Histone H3 methylated lysine-4



 structure

Last Updated ( Monday, 15 October 2007 )
 
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