1S4Z

HP1 chromo shadow domain in complex with PXVXL motif of CAF-1

Summary for 1S4Z

• Entry DOI: 10.2210/pdb1s4z/pdb
• Descriptor: Chromobox protein homolog 1, Chromatin assembly factor 1 subunit A (2 entities in total)
• Functional Keywords: gene regulation
• Biological source: Mus musculus (house mouse); More
• Cellular location: Nucleus: P23197 Q9QWF0
• Total number of polymer chains: 3
• Total formula weight: 20365.08

Authors

Thiru, A.,Nietlispach, D.,Mott, H.R.,Okuwaki, M.,Lyon, D.,Nielsen, P.R.,Hirshberg, M.,Verreault, A.,Murzina, N.V.,Laue, E.D. (deposition date: 2004-01-19, release date: 2004-03-23, Last modification date: 2024-05-22)

Primary citation

Thiru, A.,Nietlispach, D.,Mott, H.R.,Okuwaki, M.,Lyon, D.,Nielsen, P.R.,Hirshberg, M.,Verreault, A.,Murzina, N.V.,Laue, E.D.
Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin.
Embo J., 23:489-499, 2004

PubMed Abstract: HP1 family proteins are adaptor molecules, containing two related chromo domains that are required for chromatin packaging and gene silencing. Here we present the structure of the chromo shadow domain from mouse HP1beta bound to a peptide containing a consensus PXVXL motif found in many HP1 binding partners. The shadow domain exhibits a novel mode of peptide recognition, where the peptide binds across the dimer interface, sandwiched in a beta-sheet between strands from each monomer. The structure allows us to predict which other shadow domains bind similar PXVXL motif-containing peptides and provides a framework for predicting the sequence specificity of the others. We show that targeting of HP1beta to heterochromatin requires shadow domain interactions with PXVXL-containing proteins in addition to chromo domain recognition of Lys-9-methylated histone H3. Interestingly, it also appears to require the simultaneous recognition of two Lys-9-methylated histone H3 molecules. This finding implies a further complexity to the histone code for regulation of chromatin structure and suggests how binding of HP1 family proteins may lead to its condensation.

PubMed: 14765118
DOI: 10.1038/sj.emboj.7600088

Experimental method

SOLUTION NMR