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| Autor | Maofu Fu, Mahadev Rao, Kongming Wu, Chenguang Wang, Xueping Zhang, Mohamed Hessien, Yee-Guide Yeung, Daniel Gioeli, Michael J. Weber, and Richard G. Pestell |
| Titel | The Androgen Receptor Acetylation Site Regulates cAMP and AKT but Not ERK-induced Activity |
| Zeitschrift | J Biol Chem. |
| Ausgabe | 279 |
| Datum | 9. Juli 2004 |
| Nummer | 28 |
| Seiten | 29436–29449 |
| Anmerkung | Epub 2004 Apr 30 |
| DOI | 10.1074/jbc.M313466200 |
| URL | http://www.jbc.org/content/279/28/29436.full.pdf+html |
Literaturverz. |
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| Fußnoten | no |
| Fragmente | 1 |
Fragmente der Quelle:
| [1.] Rlm/Fragment 009 01 - Diskussion Zuletzt bearbeitet: 2014-12-01 17:33:22 Singulus | Fragment, Fu et al 2004, Gesichtet, KomplettPlagiat, Rlm, SMWFragment, Schutzlevel sysop |
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| Untersuchte Arbeit: Seite: 9, Zeilen: 1-12 |
Quelle: Fu et al 2004 Seite(n): 29436, Zeilen: right col. 10-24 |
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| The C-terminal region of the AR, the hinge region and ligand-binding domain (LBD) is responsible for ligand binding and receptor dimerization. The well conserved DNA binding domain consists of 68 amino acids with two zinc finger structures. In contrast to several other hormone-regulated nuclear receptors, the AR lacks an intrinsic activation function 2 in the LBD domain. The LBD domain, which consists of twelve α-helices, projects away from the hormone-binding pocket in the absence of ligand and undergoes substantial conformational changes in the presence of ligand . [sic] The folding of the most C-terminal helix 12 (H12) over the ligand-binding pocket in turn creates new structural surfaces that bind coactivators required for efficient trans-activation. | The C-terminal region of the AR, including the hinge region and ligand-binding domain (LBD) is responsible for ligand binding and dimerization. The well conserved DNA binding domain consists of 68 amino acids with two zinc finger structures. The N-terminal region contributes to transcriptional activation through its activation function 1 (2). In contrast to several other hormone-regulated nuclear receptors, the AR lacks an intrinsic activation function 2 function in the LBD. The LBD, which consists of twelve α-helices, projects away from the hormone-binding pocket in the absence of ligand and undergoes substantial conformational changes in the presence of ligand (3). The folding of the most C-terminal helix 12 (H12) over the ligand-binding pocket in turn creates new structural surfaces that bind coactivators required for efficient trans-activation.
2. Alen, P., Claessens, F., Verhoeven, G., Rombauts, W., and Peeters, B. (1999) Mol. Cell. Biol. 19, 6085–6097 3. Marhefka, C. A., Moore, B. M., 2nd, Bishop, T. C., Kirkovsky, L., Mukherjee, A., Dalton, J. T., and Miller, D. D. (2001) J. Med. Chem. 44, 1729–1740 |
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