2fmm
From Proteopedia
(New page: 200px<br /> <applet load="2fmm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fmm, resolution 1.8Å" /> '''Crystal Structure of...) |
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| - | [[Image:2fmm.gif|left|200px]]<br /> | + | [[Image:2fmm.gif|left|200px]]<br /><applet load="2fmm" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2fmm, resolution 1.8Å" /> | caption="2fmm, resolution 1.8Å" /> | ||
'''Crystal Structure of EMSY-HP1 complex'''<br /> | '''Crystal Structure of EMSY-HP1 complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Heterochromatin protein-1 (HP1) plays an essential role in both the | + | Heterochromatin protein-1 (HP1) plays an essential role in both the assembly of higher-order chromatin structure and epigenetic inheritance. The C-terminal chromo shadow domain (CSD) of HP1 is responsible for homodimerization and interaction with a number of chromatin-associated nonhistone proteins, including EMSY, which is a BRCA2-interacting protein that has been implicated in the development of breast and ovarian cancer. We have determined the crystal structure of the HP1beta CSD in complex with the N-terminal domain of EMSY at 1.8 A resolution. Surprisingly, the structure reveals that EMSY is bound by two HP1 CSD homodimers, and the binding sequences differ from the consensus HP1 binding motif PXVXL. This structural information expands our understanding of HP1 binding specificity and provides insights into interactions between HP1 homodimers that are likely to be important for heterochromatin formation. |
==About this Structure== | ==About this Structure== | ||
| - | 2FMM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2FMM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: heterochromatin protein 1]] | [[Category: heterochromatin protein 1]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:03 2008'' |
Revision as of 15:23, 21 February 2008
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Crystal Structure of EMSY-HP1 complex
Overview
Heterochromatin protein-1 (HP1) plays an essential role in both the assembly of higher-order chromatin structure and epigenetic inheritance. The C-terminal chromo shadow domain (CSD) of HP1 is responsible for homodimerization and interaction with a number of chromatin-associated nonhistone proteins, including EMSY, which is a BRCA2-interacting protein that has been implicated in the development of breast and ovarian cancer. We have determined the crystal structure of the HP1beta CSD in complex with the N-terminal domain of EMSY at 1.8 A resolution. Surprisingly, the structure reveals that EMSY is bound by two HP1 CSD homodimers, and the binding sequences differ from the consensus HP1 binding motif PXVXL. This structural information expands our understanding of HP1 binding specificity and provides insights into interactions between HP1 homodimers that are likely to be important for heterochromatin formation.
About this Structure
2FMM is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the HP1-EMSY complex reveals an unusual mode of HP1 binding., Huang Y, Myers MP, Xu RM, Structure. 2006 Apr;14(4):703-12. PMID:16615912
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