Transcriptional cooperativity: bending over backwards and doing the flip
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Updated: Aug 14, 2026

High-throughput Purification of Affinity-tagged Recombinant Proteins
Published on: August 26, 2012
1Howard Hughes Medical Institute, University of Michigan Medical School, Ann Arbor 48109-0650, USA. kerppola@umich.edu
Abstract:
The structures of the NFAT1-Fos-Jun-ARRE2 and MAT alpha 2-MCM1-STE6 transcription regulatory complexes reveal changes in protein conformation and DNA bending. Studies of the interaction between Fos-Jun and NFAT1 in solution corroborate the crystallographic analysis. These results manifest the flexibility required for cooperative binding to composite regulatory elements.
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