Backbone resonance assignment of the BCL6-BTB?POZ domain.pdf (827.31 kB)
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Backbone resonance assignment of the BCL6-BTB/POZ domain

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posted on 03.05.2018, 15:40 by Li-Ying Lin, S. E. Evans, Louise Fairall, John W. R. Schwabe, Simon D. Wagner, Frederick W. Muskett
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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Citation

Biomolecular NMR Assignments, 2018, 12 (1), pp. 47-50

Author affiliation

/Organisation/COLLEGE OF LIFE SCIENCES/Biological Sciences/Molecular & Cell Biology

Version

VoR (Version of Record)

Published in

Biomolecular NMR Assignments

Publisher

Springer Verlag

issn

1874-2718

eissn

1874-270X

Acceptance date

13/09/2017

Copyright date

2017

Available date

03/05/2018

Publisher version

https://link.springer.com/article/10.1007/s12104-017-9778-z

Language

en

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