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. 2001 Dec;8(6):1267-76.
doi: 10.1016/s1097-2765(01)00410-5.

Structural studies of Ets-1/Pax5 complex formation on DNA

C W Garvie  1 , J Hagman, C Wolberger
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Free article

Structural studies of Ets-1/Pax5 complex formation on DNA

C W Garvie et al. Mol Cell. 2001 Dec.
Free article

Abstract

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.

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