Promise

Our promise to you: Guaranteed product quality, expert customer support.

Eed Protein Crystal(CBCRY07)

Product Summary
Name Eed Protein Crystal Download Datasheet
Background
Background The crystal structure of EED in complex with a 30 residue peptide from EZH2 reveals that the peptide binds to the bottom of the WD-repeat domain of EED. The structural determinants of EZH2-EED interaction are present not only in EZH2 and EZH1 but also in its Drosophila homolog E(Z), suggesting that the recognition of ESC by E(Z) in Drosophila employs similar structural motifs. Structure-based mutagenesis identified critical residues from both EED and EZH2 for their interaction.
Molecular Description
Protein Classificationgene regulation
Structure Weight45399.05 Da
Polymer1
MoleculeEmbryonic ectoderm development
Chain Length361 amino acids
Polymer2
MoleculeEnhancer of zeste homolog 2
Chain Length30 amino acids
Crystal Description
PDB ID2QXV
MMDB ID59571
SourceE.coli
MethodX-Ray Diffraction
Resolution1.82 Å
Gene Information
Gene NameEed
Synonymsembryonic ectoderm development; ENSMUSG00000039373; l(7)5Rn; l7Rn5; lusk; OTTMUSP00000023294; lethal; Chr 7; Rinchik 5
Gene ID13626
Chromosome Location7
Functionchromatin binding; histone methyltransferase binding; protein binding
Gene NameEzh2
Synonymsenhancer of zeste homolog 2 (Drosophila); Enx-1, Enx1h, KIAA4065, KMT6; MGC90723; mKIAA4065; OTTMUSP00000023406; enhancer of zeste homolog 2; heed; wd protein associating with integrin cytoplasmic t; wait1; wd protein associating with integrin cytoplasmic tails 1
Gene ID14056
Chromosome Location6 19.2 cM
Functionchromatin binding; histone methyltransferase binding; protein binding
Reference
Reference Han, Z., Xing, X., Hu, M., Zhang, Y., Liu, P., Chai, J. (2007) Structural basis of EZH2 recognition by EED Structure 15: 1306-1315

Online Inquiry

  • Verification code
    Click image to refresh the verification code.