한국자기공명학회논문지 (Journal of the Korean Magnetic Resonance Society)

한국자기공명학회 (Korean Magnetic Resonance Society)
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Backbone assignment of HMGB1 A-box and molecular interaction with Hoxc9DBD studied by paramagnetic probe

  • Choi, Ji Woong (College of Pharmacy and Gachon Institute of Pharmaceutical Sciences, Gachon University) ;
  • Park, Sung Jean (College of Pharmacy and Gachon Institute of Pharmaceutical Sciences, Gachon University)
  • 투고 : 2021.05.28
  • 심사 : 2021.06.07
  • 발행 : 2021.06.20
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초록

High mobility group protein B1 (HMGB1) is a highly conserved, non-histone, chromatin associated nuclear protein encoded by HMGB1 gene. HMGB1 proteins may be general co-factors in Hox-mediated transcriptional activation that facilitate the access of Hox proteins to specific DNA targets. It is unclear that the exact binding interface of Hoxc9DBD and HMGB1. To identify the interface and binding affinity of Hoxc9DBD and HMGB1 A-box, the paramagnetic probe, MTSL was used in NMR titration experiment. It is attached to the N-terminal end of HMGB1 A-box by reaction with thiol groups. The backbone assignment of HMGB1 A-box was achieved with 3D NMR techinques. The 15N-labeled HMGB1 A-box was titrated with MTSL-labeled Hoxc9DBD respectively. Based on the chemical shift changes we can identify the interacting residues and further map out the binding sites on the protein structure. The NMR titration result showed that the binding interface of HMGB1 A-box is around loop-1 between helix-1 and helix-2. In addition, the additional contacts were found in N- and C-terminus. The N-terminal arm region of Hoxc9DBD is the major binding region and the loop between helix1 and helix2 is the minor binding region.

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과제정보

This work was supported by the Gachon University research fund of 2019 (GCU-2019-0707).This research was also supported by the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science, and Technology (2018R1D1A1B07050426) The authors thank the high field NMR facility at the Korea Basic Science Institute and the National Center for Inter-university Research Facilities.

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