Cat. No.

CBCRY07

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 Classification

gene regulation

Structure Weight

45399.05 Da

Polymer

1

Molecule

Embryonic ectoderm development

Chain Length

361 amino acids

Polymer

2

Molecule

Enhancer of zeste homolog 2  

Chain Length

30 amino acids

Crystal Description

PDB ID

2QXV

MMDB ID

59571

Source

E.coli

Method

X-Ray Diffraction

Resolution

1.82 Å

Gene information

Gene Name

Eed

Synonyms

embryonic ectoderm development; ENSMUSG00000039373; l(7)5Rn; l7Rn5; lusk; OTTMUSP00000023294; lethal; Chr 7; Rinchik 5

GeneID

13626

Chromosome  Location

7

Function

chromatin binding; histone methyltransferase binding; protein binding

Gene Name

Ezh2

Synonyms

enhancer 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

GeneID

14056

Chromosome  Location

6 19.2 cM

Function

DNA binding; chromatin binding; histone methyltranferase activity; methyltransferase; protein binding; transferase activity.

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