2FMM

Crystal Structure of EMSY-HP1 complex

Summary for 2FMM

• Entry DOI: 10.2210/pdb2fmm/pdb
• Descriptor: Protein EMSY, Chromobox protein homolog 1, SULFATE ION, ... (4 entities in total)
• Functional Keywords: ent domain, chromo shadow domain, emsy protein, heterochromatin protein 1, transcription
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q7Z589 P83916
• Total number of polymer chains: 5
• Total formula weight: 48456.46

Authors

Huang, Y. (deposition date: 2006-01-09, release date: 2006-05-23, Last modification date: 2024-02-14)

Primary citation

Huang, Y.,Myers, M.P.,Xu, R.M.
Crystal structure of the HP1-EMSY complex reveals an unusual mode of HP1 binding.
Structure, 14:703-712, 2006

PubMed Abstract: 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.

PubMed: 16615912
DOI: 10.1016/j.str.2006.01.007

Experimental method

X-RAY DIFFRACTION (1.8 Å)