Structural and functional analysis of domains of the progesterone receptor

作者: Krista K. Hill , Sarah C. Roemer , Mair E.A. Churchill , Dean P. Edwards

DOI: 10.1016/J.MCE.2011.07.017

关键词:

摘要: 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) hinge region between LBD DBD. The is more than just a flexible DBD capable co-regulatory minor groove flanking response elements. Because can directly participate in it has also been termed carboxyl terminal extension (CTE) domain. CTE NTD dynamic receptor that adopt multiple conformations depending on environment interacting DNA. Both have important regulatory roles for functions related to ability form active conformations. This review focuses studies progesterone (PR), well work with steroid/nuclear receptors.

参考文章(140)
M. E. Meyer, A. Pornon, J. W. Ji, M. T. Bocquel, P. Chambon, H. Gronemeyer, Agonistic and antagonistic activities of RU486 on the functions of the human progesterone receptor. The EMBO Journal. ,vol. 9, pp. 3923- 3932 ,(1990) , 10.1002/J.1460-2075.1990.TB07613.X
M.E. Meyer, C Quirin-Stricker, T Lerouge, M.T. Bocquel, H Gronemeyer, A limiting factor mediates the differential activation of promoters by the human progesterone receptor isoforms. Journal of Biological Chemistry. ,vol. 267, pp. 10882- 10887 ,(1992) , 10.1016/S0021-9258(19)50100-4
G.F. Allan, X Leng, S.Y. Tsai, N.L. Weigel, D.P. Edwards, M.J. Tsai, B.W. O'Malley, Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation. Journal of Biological Chemistry. ,vol. 267, pp. 19513- 19520 ,(1992) , 10.1016/S0021-9258(18)41805-4
P. Kastner, A. Krust, B. Turcotte, U. Stropp, L. Tora, H. Gronemeyer, P. Chambon, Two distinct estrogen‐regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B. The EMBO Journal. ,vol. 9, pp. 1603- 1614 ,(1990) , 10.1002/J.1460-2075.1990.TB08280.X
Jeffrey A. Lefstin, Keith R. Yamamoto, Allosteric effects of DNA on transcriptional regulators. Nature. ,vol. 392, pp. 885- 888 ,(1998) , 10.1038/31860
A Aronheim, E Zandi, H Hennemann, S J Elledge, M Karin, Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions. Molecular and Cellular Biology. ,vol. 17, pp. 3094- 3102 ,(1997) , 10.1128/MCB.17.6.3094
Shawn P. Williams, Paul B. Sigler, Atomic structure of progesterone complexed with its receptor. Nature. ,vol. 393, pp. 392- 396 ,(1998) , 10.1038/30775
Byung-Chul Jeong, Cheol Yi Hong, Soma Chattopadhyay, Jin Hee Park, Eun-Yeung Gong, Hyun-Jin Kim, Sang-Young Chun, Keesook Lee, Androgen Receptor Corepressor-19 kDa (ARR19), a Leucine-Rich Protein that Represses the Transcriptional Activity of Androgen Receptor through Recruitment of Histone Deacetylase Molecular Endocrinology. ,vol. 18, pp. 13- 25 ,(2004) , 10.1210/ME.2003-0065
Larry N. Petz, Ann M. Nardulli, Jongsook Kim, Kathryn B. Horwitz, Leonard P. Freedman, David J. Shapiro, DNA bending is induced by binding of the glucocorticoid receptor DNA binding domain and progesterone receptors to their response element The Journal of Steroid Biochemistry and Molecular Biology. ,vol. 60, pp. 31- 41 ,(1997) , 10.1016/S0960-0760(96)00171-9
Hany Abdel-Hafiz, Glenn S. Takimoto, Lin Tung, Kathryn B. Horwitz, The inhibitory function in human progesterone receptor N termini binds SUMO-1 protein to regulate autoinhibition and transrepression. Journal of Biological Chemistry. ,vol. 277, pp. 33950- 33956 ,(2002) , 10.1074/JBC.M204573200