JKMRS Volume 22, No 1, pp 18; Backbone Dynamics and Model-Free... | |
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2018년 03월 20일 / 조회수: 640 | |
Backbone Dynamics
and Model-Free Analysis of N-terminal Domain of Human Replication Protein A 70
Sooji
Yoo and Chin-Ju Park*
Department of Chemistry, Gwangju Institute of Science
and Technology, Gwangju 61005, South Korea
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 15N
relaxation parameters (T1, T2
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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첨부파일 | 3-JKMRS_박진주.pdf |