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Eed Protein Crystal

(CBCRY07)  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 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
Gene ID
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
Gene ID
14056
Chromosome Location
6 19.2 cM
Function
chromatin 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