|作者：||Larry N. Petz, Ann M. Nardulli, Jongsook Kim, Kathryn B. Horwitz, Leonard P. Freedman, David J. Shapiro|
1Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, U.S.A.
2Department of Molecular and Integrative Physiology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, U.S.A.
3Department of Medicine, University of Colorado Health Sciences Center, Denver, CO 80262, U.S.A.
4Department of Pathology, University of Colorado Health Sciences Center, Denver, CO 80262, U.S.A.
5Cell Biology and Genetics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, U.S.A.
|刊名：||Journal of Steroid Biochemistry and Molecular Biology, 1997, Vol.60 (1), pp.31-41|
|原始语种摘要：||Abstract(#br)Circular permutation analysis was used to determine the degree of DNA bending induced by binding of the glucocorticoid receptor (GR) DNA binding domain (DBD), the human progesterone receptor (PR) DBD, PR-A:A and PR-B:B homodimers, and PR-A:B heterodimers to the glucocorticoid response element/progesterone response element ( GRE PRE ). The bending angles induced by the GR DBD and the PR DBD were approximately 28° and 25°, respectively. The PR-B:B and PR-A:A homodimers and the PR-A:B heterodimers all induced similar DNA bending angles of 72–77°. The substantially greater DNA bend induced by full-length PR compared to the PR DBD indicates that sequences outside the classic zinc finger DNA binding domain may play an important role in the interaction of PR with the GRE PRE .... Because PR-A:A and PR-B:B homodimers and the PR-A:B heterodimers induce similar DNA bends, the different abilities of the PR-A and PR-B isoforms to activate transcription are not due to differences in their abilities to distort DNA structure.|