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No Image The CSD/SC structure appears as a three-stranded antiparallel b-sheet followed by two a-helices. This closely resembles the chromodomain, but with two helices separated by a proline residue induced turn in place of the single a-helix of the chromodomain. Unlike the chromodomain, the CSD allows dimerization via interaction of the H2 helices. Dimerization of CSDs produces a hydrophobic pit capable of accommodating conserved hydrophobic pentapeptide motif (PXVXL) found in CSD interacting proteins. The figure shows the structure of the CSD of Swi6 as a monomer.

Structure Reference:
Cowieson, NP. et al. (2000) Curr. Biol. 10(9): 517-525. PDB: 1E0B.

Domain binding and function:
 structure The Shadow Chromo Domain (CSD) is a 40 to 70 amino acid domain that occurs only in the context of proteins containing a chromodomain (CD). While the Shadow Chromodomain resembles the Chromodomain structurally, it appears to function in a distinct manner with respect to protein-protein interactions. The CSD lacks the hydrophobic sash believed to mediate CD interactions. Shadow Chromo domains form stable dimers and dimerization generates an interaction pit that may allow docking with partner proteins containing an extended hydrophobic pentapeptide motif.
Examples of Proteins: 
SCD domain protein
Binding partner
Swi6 homotypic interaction
HP1 Ku70, Su(var)3-7

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