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The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18. 总被引:42,自引:7,他引:35 下载免费PDF全文
B Le Douarin C Zechel J M Garnier Y Lutz L Tora P Pierrat D Heery H Gronemeyer P Chambon R Losson 《The EMBO journal》1995,14(9):2020-2033
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Slagsvold T Kraus I Bentzen T Palvimo J Saatcioglu F 《Molecular endocrinology (Baltimore, Md.)》2000,14(10):1603-1617
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Estrogen receptor pathways to AP-1 总被引:21,自引:0,他引:21
Kushner PJ Agard DA Greene GL Scanlan TS Shiau AK Uht RM Webb P 《The Journal of steroid biochemistry and molecular biology》2000,74(5):311-317
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Functional properties of the N-terminal region of progesterone receptors and their mechanistic relationship to structure 总被引:7,自引:0,他引:7
Takimoto GS Tung L Abdel-Hafiz H Abel MG Sartorius CA Richer JK Jacobsen BM Bain DL Horwitz KB 《The Journal of steroid biochemistry and molecular biology》2003,85(2-5):209-219
Progesterone receptors (PR) are present in two isoforms, PR-A and PR-B. The B-upstream segment (BUS) of PR-B is a 164 amino acid N-terminal extension that is missing in PR-A and is responsible for the functional differences reported between the two isoforms. BUS contains an activation function (AF3) which is defined by a core domain between residues 54–154 whose activity is dependent upon a single Trp residue and two LXXLL motifs. We have also identified sites both within and outside of BUS that repress the strong synergism between AF3 and AF1 in the N-terminal region and AF2 in the hormone binding domain. One of these repressor sites is a consensus binding motif for the small ubiquitin-like modifier protein, SUMO-1 (387IKEE). The DNA binding domain (DBD) structure is also important for function. When BUS is linked to the glucocorticoid receptor DBD, AF3 activity is substantially attenuated, suggesting that binding to a DNA response element results in allosteric communication between the DBD and N-terminal functional regions. Lastly, biochemical and biophysical analyses of highly purified PR-B and PR-A N-terminal regions reveal that they are unstructured unless the DBD is present. Thus, the DBD stabilizes N-terminal structure. We propose a model in which the DBD through DNA binding, and BUS through protein–protein interactions, stabilize active receptor conformers within an ensemble distribution of active and inactive conformational states. This would explain why PR-B are stronger transactivators than PR-A. 相似文献