The nuclear receptor corepressor (N-CoR) contains three isoleucine motifs (I/LXXII) that serve as receptor interaction domains (IDs).
The nuclear receptor corepressor (N-CoR) contains three isoleucine motifs (I/LXXII) that serve as receptor interaction domains (IDs).
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核受体辅阻遏物 (N-CoR) 包含三个异亮氨酸基序 (I/LXXII)，用作受体相互作用域 (ID)。
DOI：
10.1210/mend.14.12.0566
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发表时间：
2000
影响因子：
--
通讯作者：
P. Kushner
中科院分区：
文献类型：
--
作者：
P. Webb;C. Anderson;Cathleen D. Valentine;Phuong H. Nguyen;A. Marimuthu;B. West;J. Baxter;P. Kushner
Unliganded thyroid hormone receptors (TRs) repress transcription through recruitment of corepressors, including nuclear receptor corepressor (N-CoR). We find that N-CoR contains three interaction domains (IDs) that bind to TR, rather than the previously reported two. The hitherto unrecognized ID (ID3) serves as a fully functional TR binding site, both in vivo and in vitro, and may be the most important for TR binding. Each ID motif contains a conserved hydrophobic core (I/LXXII) that resembles the hydrophobic core of nuclear receptor boxes (LXXLL), which mediates p160 coactivator binding to liganded nuclear receptors. Although the integrity of the I/LXXII motif is required for ID function, substitution of ID isoleucines with leucines did not allow ID peptides to bind to liganded TR, and substitution of NR box leucines with isoleucines did not allow NR box peptides to bind unliganded TR. This indicates that the binding preferences of N-CoR for unliganded TR and p160s for liganded TR are not dictated solely by the identity of conserved hydrophobic residues within their TR binding motifs. Examination of sequence conservation between IDs, and mutational analysis of individual IDs, suggests that they are comprised of the central hydrophobic core and distinct adjacent sequences that may make unique contacts with the TR surface. Accordingly, a hybrid peptide that contains distinct adjacent sequences from ID3 and ID1 shows enhanced binding to TR.
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影响因子：
16
作者：
Laherty, CD;Billin, AN;Eisenman, RN
通讯作者：
Eisenman, RN
影响因子：
--
作者：
Xiu Fen Ding;Carol M. Anderson;Han Ma;H. Hong;R. M. Uht;Peter J. Kushner;M. Stallcup
通讯作者：
Xiu Fen Ding;Carol M. Anderson;Han Ma;H. Hong;R. M. Uht;Peter J. Kushner;M. Stallcup
影响因子：
--
作者：
S. Sande;M. Privalsky
通讯作者：
S. Sande;M. Privalsky
影响因子：
56.9
作者：
Feng, WJ;Ribeiro, RCJ;West, BL
通讯作者：
West, BL
核激素受体辅阻遏物 RIP13/N-CoR 中的两个受体相互作用结构域。
DOI：
10.1210/mend.10.12.8961273
发表时间：
1996
期刊：
Molecular endocrinology (Baltimore, Md.)
影响因子：
--
作者：
Seol,W;Mahon,MJ;Lee,YK;Moore,DD
通讯作者：
Moore,DD