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- W2087437874 endingPage "429" @default.
- W2087437874 startingPage "418" @default.
- W2087437874 abstract "Steroid hormone receptors are multi-domain proteins composed of conserved well-structured regions, such as ligand (LBD) and DNA binding domains (DBD), plus other naturally unstructured regions including the amino-terminal domain (NTD) and the hinge region between the LBD and DBD. The hinge is more than just a flexible region between the DBD and LBD and is capable of binding co-regulatory proteins and the minor groove of DNA flanking hormone response elements. Because the hinge can directly participate in DNA binding it has also been termed the carboxyl terminal extension (CTE) of the DNA binding domain. The CTE and NTD are dynamic regions of the receptor that can adopt multiple conformations depending on the environment of interacting proteins and DNA. Both regions have important regulatory roles for multiple receptor functions that are related to the ability of the CTE and NTD to form multiple active conformations. This review focuses on studies of the CTE and NTD of progesterone receptor (PR), as well as related work with other steroid/nuclear receptors." @default.
- W2087437874 created "2016-06-24" @default.
- W2087437874 creator A5003899589 @default.
- W2087437874 creator A5026980902 @default.
- W2087437874 creator A5029150600 @default.
- W2087437874 creator A5083507934 @default.
- W2087437874 date "2012-01-01" @default.
- W2087437874 modified "2023-09-26" @default.
- W2087437874 title "Structural and functional analysis of domains of the progesterone receptor" @default.
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