Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

Crystal structure of the human Pax6 paired domain-DNA complex reveals specific roles for the linker region and carboxy-terminal subdomain in DNA binding

Crystal structure of the human Pax6 paired domain-DNA complex reveals specific roles for the... Downloaded from genesdev.cshlp.org on November 22, 2021 - Published by Cold Spring Harbor Laboratory Press Crystal structure of the human Pax6 paired domain–DNA complex reveals specific roles for the linker region and carboxy-terminal subdomain in DNA binding 1 1 1 2 2 H. Eric Xu, Mark A. Rould, Wenqing Xu, Jonathan A. Epstein, Richard L. Maas, 1,3 and Carl O. Pabo Department of Biology and Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 USA; Genetics Division, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, Massachusetts 02115 USA Pax6, a transcription factor containing the bipartite paired DNA-binding domain, has critical roles in development of the eye, nose, pancreas, and central nervous system. The 2.5 Å structure of the human Pax6 paired domain with its optimal 26-bp site reveals extensive DNA contacts from the amino-terminal subdomain, the linker region, and the carboxy-terminal subdomain. The Pax6 structure not only confirms the docking arrangement of the amino-terminal subdomain as seen in cocrystals of the Drosophila Prd Pax protein, but also reveals some interesting differences in this region and helps explain the sequence specificity of paired domain–DNA recognition. In addition, this structure gives the first detailed information about http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Genes & Development Unpaywall

Crystal structure of the human Pax6 paired domain-DNA complex reveals specific roles for the linker region and carboxy-terminal subdomain in DNA binding

Xu, H. E.; Rould, M. A.; Xu, W.; Epstein, J. A.; Maas, R. L.; Pabo, C. O.
Genes & Development – May 15, 1999
Download PDF
14 pages

Loading next page...
 
/lp/unpaywall/crystal-structure-of-the-human-pax6-paired-domain-dna-complex-reveals-HvLhkGDiNc

References

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

Publisher
Unpaywall
ISSN
0890-9369
DOI
10.1101/gad.13.10.1263
Publisher site
See Article on Publisher Site

Abstract

Downloaded from genesdev.cshlp.org on November 22, 2021 - Published by Cold Spring Harbor Laboratory Press Crystal structure of the human Pax6 paired domain–DNA complex reveals specific roles for the linker region and carboxy-terminal subdomain in DNA binding 1 1 1 2 2 H. Eric Xu, Mark A. Rould, Wenqing Xu, Jonathan A. Epstein, Richard L. Maas, 1,3 and Carl O. Pabo Department of Biology and Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 USA; Genetics Division, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, Massachusetts 02115 USA Pax6, a transcription factor containing the bipartite paired DNA-binding domain, has critical roles in development of the eye, nose, pancreas, and central nervous system. The 2.5 Å structure of the human Pax6 paired domain with its optimal 26-bp site reveals extensive DNA contacts from the amino-terminal subdomain, the linker region, and the carboxy-terminal subdomain. The Pax6 structure not only confirms the docking arrangement of the amino-terminal subdomain as seen in cocrystals of the Drosophila Prd Pax protein, but also reveals some interesting differences in this region and helps explain the sequence specificity of paired domain–DNA recognition. In addition, this structure gives the first detailed information about

Journal

Genes & Development – Unpaywall

Published: May 15, 1999

There are no references for this article.