1s4z
From Proteopedia
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HP1 chromo shadow domain in complex with PXVXL motif of CAF-1
Overview
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.
About this Structure
1S4Z is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin., Thiru A, Nietlispach D, Mott HR, Okuwaki M, Lyon D, Nielsen PR, Hirshberg M, Verreault A, Murzina NV, Laue ED, EMBO J. 2004 Feb 11;23(3):489-99. Epub 2004 Feb 5. PMID:14765118
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