Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2009 May 21;37(13):4341–4352. doi: 10.1093/nar/gkp307

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2009 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Figure 8. — Model for the differential regulation of the Stromelysin-1 promoter by p51 and p42 Ets-1 isoforms. The binding of one p42 molecule on the EBS palindrome (core consensus motifs in green) induced DNA minor groove bending. Two p42 molecules are unable to bind the EBS palindrome due to steric clashes between the two DBD domains (DBD, in blue). In contrast, two p51 are able to overcome these steric hindrances through a cooperative interaction leading to (i) a drastic rearrangement of the inhibitory module (CtID, red diamond and NtID, red trapezoid) and the creation of an intermolecular interface between the N-terminal inhibitory domains (NtID, red trapezoid) (ii) the induction of major DNA bending (opposite to the protein–DNA interface). This ternary complex, via the induced specific DNA curvature, is responsible for the full transactivation of the promoter.