Backbone resonance assignment of the BCL6-BTB/POZ domain.
Backbone resonance assignment of the BCL6-BTB/POZ domain.
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DOI:
10.1007/s12104-017-9778-z
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发表时间:
2018-04
影响因子:
0.9
通讯作者:
Muskett FW
中科院分区:
文献类型:
--
作者:
Lin LY;Evans SE;Fairall L;Schwabe JWR;Wagner SD;Muskett FW
BCL6 is a transcriptional repressor. Two domains of the protein, the N-terminal BTB-POZ domain and the RD2 domain are responsible for recruitment of co-repressor molecules and histone deacetylases. The BTB-POZ domain is found in a large and diverse range of proteins that play important roles in development, homeostasis and neoplasia. Crystal structures of several BTB-POZ domains, including BCL6 have been determined. The BTB-POZ domain of BCL6 not only mediates dimerisation but is also responsible for recruitment of co-repressors such as SMRT, NCOR and BCOR. Interestingly both SMRT and BCOR bind to the same site within the BCL6 BTB-POZ domain despite having very different primary sequences. Since both peptides and small molecules have been shown to bind to the co-repressor binding site it would suggest that the BTB_POZ domain is a suitable target for drug discovery. Here we report near complete backbone 15N, 13C and 1H assignments for the BTB-POZ domain of BCL6 to assist in the analysis of binding modes for small molecules.
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影响因子:
2.7
作者:
DELAGLIO, F;GRZESIEK, S;BAX, A
通讯作者:
BAX, A
DOI:
10.1073/pnas.94.20.10762
发表时间:
1997-09-30
影响因子:
11.1
作者:
Dhordain, P;Albagli, O;Leprince, D
通讯作者:
Leprince, D
影响因子:
16
作者:
Ghetu, Alexandru F.;Corcoran, Connie M.;Prive, Gilbert G.
通讯作者:
Prive, Gilbert G.
影响因子:
50.3
作者:
Cattoretti, G;Pasqualucci, L;Dalla-Favera, R
通讯作者:
Dalla-Favera, R
影响因子:
3.7
作者:
Evans SE;Goult BT;Fairall L;Jamieson AG;Ko Ferrigno P;Ford R;Schwabe JW;Wagner SD
通讯作者:
Wagner SD