2fmm | pdb_00002fmm
From Proteopedia
Crystal Structure of EMSY-HP1 complex
| ||||||||||||
Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHeterochromatin 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
Contents | ||||||||||||||||||||
This page was last modified 10:50, 30 September 2014.