Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)

Korean Magnetic Resonance Society (한국자기공명학회)
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Backbone Dynamics and Model-Free Analysis of N-terminal Domain of Human Replication Protein A 70

  • Yoo, Sooji (Department of Chemistry, Gwangju Institute of Science and Technology) ;
  • Park, Chin-Ju (Department of Chemistry, Gwangju Institute of Science and Technology)
  • Received : 2018.01.30
  • Accepted : 2018.03.04
  • Published : 2018.03.20
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Abstract

Replication protein A (RPA) is an essential single-stranded DNA binding protein in DNA processing. It is known that N terminal domain of RPA70 (RPA70N) recruits various protein partners including damage-response proteins such as p53, ATRIP, Rad9, and MRE11. Although the common binding residues of RPA70N were revealed, dynamic properties of the protein are not studied yet. In this study, we measured $^{15}N$ relaxation parameters ($T_1,\;T_2$ and heteronuclear NOE) of human RPA70N and analyzed them using model-free analysis. Our data showed that the two loops near the binding site experience fast time scale motion while the binding site does not. It suggests that the protein binding surface of RPA70N is mostly rigid for minimizing entropy cost of binding and the loops can experience conformational changes.

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References

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