NMR studies on the structure of XPC bindign domain of hHR23B protein = NMR을 이용한 hHR23B 단백질의 XPC binding domain의 구조연구

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The initiation mechanism of the recognizing a damaged DNA was the key issue in the Nucleotide Excision Repair (NER) pathway. Several studies have found that damaged DNA was first recognized by XPC-hHR23B proteins. XPC-hHR23B complex enhanced the binding activity to the damaged DNA than the XPC alone. The functionally characterized XPC-binding domain of hHR23B(277-332) has been identified in vitro NER reaction. In this study the structure of hHR23B(275-342) was first solved with heteronuclear triple resonance NMR spectroscopy. To bock the aggregation of XPC binding domain of hHR23B(277-332), N-terminally 3 residues and C-terminally Gly-rich loop was additionally expanded in cloning strategy. For the 3D NMR structure study, 1mM hHR23B(275-342) was concentrated and 10mM CHAPS must be added for the blocking from the non-specific interactions among the samples or from oligomerization. The solution structure of XPC binding domain of hHR23B shows that 4 helical bundles which have tightly interacted with hydrophobic core residues. The conserved amino acids of XPC binding domain between hHR23B, hHR23A and hPLICs revealed that most Pro residues shows structurally expected characters to make helix kinked and turned. Two hydrophobic surfaces were also detected with electrostatic potential surface analysis in the structure of XPC binding domain of hHR23B. One of two or both of them would be served as the directly interaction surface with XPC. Additionally with the N-terminally helix favorable domain (Helix 0) with hydrophobic patch between Helix 1, 2, 3 region will be involved in the XPC binding mode. Relaxation study of the XPC binding domain of hHR23B show that four helices are rigid but N-terminal helix favorable residues show anisotropic internal motion. Between the Helix0 and Helix 1 parts, XPC binding domain of hHR23B has more flexible and turn motion. From this dynamics characters the Helix 0 and Helix 1 could stimulate the DNA binding mode of XPC. From the Dali ser...
Advisors
Choi, Byong-Seokresearcher최병석researcher
Description
한국과학기술원 : 화학과,
Publisher
한국과학기술원
Issue Date
2003
Identifier
231036/325007  / 000985059
Language
eng
Description

학위논문(박사) - 한국과학기술원 : 화학과, 2003.8, [ viii, 79 p. ]

Keywords

hHR23B; damaged DNA; NMR; protein structure; XOC; XPC; hHR23B; damaged DNA; NMR; 단백질구조

URI
http://hdl.handle.net/10203/31614
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=231036&flag=dissertation
Appears in Collection
CH-Theses_Ph.D.(박사논문)
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