Crystal Structure of the HP1-EMSY Complex Reveals an Unusual Mode of HP1 Binding

Journal Article · Sun Jan 01 04:00:00 EST 2006 · Structure

DOI:https://doi.org/10.1016/j.str.2006.01.007· OSTI ID:914308

Huang, Y; Myers, M; Xu, R

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 HP1{beta} CSD in complex with the N-terminal domain of EMSY at 1.8 Angstroms 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.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 914308
• Report Number(s): BNL--78876-2007-JA
• Journal Information: Structure, Journal Name: Structure Journal Issue: 4 Vol. 14
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
CHROMATIN
CRYSTAL STRUCTURE
HETEROCHROMATIN
MAMMARY GLANDS
NEOPLASMS
PROTEINS
RESOLUTION
SPECIFICITY
national synchrotron light source