Summary information and primary citation

1k7a; DSSR-derived features in text and JSON formats
X-ray (2.8 Å)
Ets-1(331-440)+ggag duplex
Garvie CW, Hagman J, Wolberger C (2001): "Structural studies of Ets-1/Pax5 complex formation on DNA." Mol.Cell, 8, 1267-1276. doi: 10.1016/S1097-2765(01)00410-5.
Pax5 regulates the B cell-specific expression of the mb-1 gene together with members of the Ets family of transcriptional activators. The Ets proteins on their own bind poorly to the Pax5/Ets binding site, but can be recruited to the site by cooperative interactions with Pax5. The structure of the ETS domain of Ets-1 and the paired domain of Pax5 bound to DNA reveals the molecular details of the selective recruitment of different Ets proteins by Pax5. Comparison with structures of Ets-1 alone bound to both high- and low-affinity DNA sites reveals that Pax5 alters the Ets-1 contacts with DNA. The ability of one protein to alter the DNA sequence-specific contacts of another provides a general mechanism for combinatorial regulation of transcription.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js