The bZIP Targets Overlapping DNA Subsites within a Half-Site, Resulting in Increased Binding Affinities-Reference-Cited by-同舟云学术

The bZIP Targets Overlapping DNA Subsites within a Half-Site, Resulting in Increased Binding Affinities

Published:2008-08-15 Issue:36 Volume:47 Page:9646-9652
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Chan I-San¹,Shahravan S. Hesam¹,Fedorova Anna V.¹,Shin Jumi A.¹

Affiliation:

1. Department of Chemistry, University of Toronto, Mississauga, Ontario, Canada L5L 1C6, and Institute of Biomaterials and Biomedical Engineering, University of Toronto, Toronto, Ontario, Canada M5S 3G9

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi800355t

Reference23 articles.

1. Helix-turn-helix, zinc-finger, and leucine-zipper motifs for eukaryotic transcriptional regulatory proteins

2. The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins

3. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α Helices: Crystal structure of the protein-DNA complex

4. The X-ray Structure of the GCN4-bZIP Bound to ATF/CREB Site DNA Shows the Complex Depends on DNA Flexibility

5. Crystal Structure of a bZIP/DNA Complex at 2.2 Å: Determinants of DNA Specific Recognition

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1. The bZIP Dimer Localizes at DNA Full-Sites Where Each Basic Region Can Alternately Translocate and Bind to Subsites at the Half-Site;Biochemistry;2012-08-10

2. The Basic Helix−Loop−Helix Region of Human Neurogenin 1 Is a Monomeric Natively Unfolded Protein Which Forms a “Fuzzy” Complex upon DNA Binding;Biochemistry;2010-02-08