1s4z
From Proteopedia
(New page: 200px<br /> <applet load="1s4z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s4z" /> '''HP1 chromo shadow domain in complex with PX...) |
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'''HP1 chromo shadow domain in complex with PXVXL motif of CAF-1'''<br /> | '''HP1 chromo shadow domain in complex with PXVXL motif of CAF-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | HP1 family proteins are adaptor molecules, containing two related chromo | + | 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== | ==About this Structure== | ||
| - | 1S4Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1S4Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Hirshberg, M.]] | [[Category: Hirshberg, M.]] | ||
| - | [[Category: Laue, E | + | [[Category: Laue, E D.]] |
[[Category: Lyon, D.]] | [[Category: Lyon, D.]] | ||
| - | [[Category: Mott, H | + | [[Category: Mott, H R.]] |
| - | [[Category: Murzina, N | + | [[Category: Murzina, N V.]] |
| - | [[Category: Nielsen, P | + | [[Category: Nielsen, P R.]] |
[[Category: Nietlispach, D.]] | [[Category: Nietlispach, D.]] | ||
[[Category: Okuwaki, M.]] | [[Category: Okuwaki, M.]] | ||
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[[Category: gene regulation]] | [[Category: gene regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:58 2008'' |
Revision as of 12:57, 21 February 2008
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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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