Uncorrelated Effect of Interdomain Contact on Pin1 Isomerase Activity Reveals Positive Catalytic Cooperativity | |
Yang, Yunhuang2; Zhu, Jiang2; Liu, Maili1,2; Li, Ying2; Zhu, Wenkai1,2 | |
刊名 | JOURNAL OF PHYSICAL CHEMISTRY LETTERS |
2019-03-21 | |
卷号 | 10期号:6页码:1272-1278 |
ISSN号 | 1948-7185 |
DOI | 10.1021/acs.jpclett.9b00052 |
英文摘要 | Pin1 is a two-domain peptidyl-prolyl isomerase (PPIase) associated with neurodegeneration and tumorigenesis. The two domains, a WW and a PPIase domain, are connected by a flexible linker, making Pin1 adopt various conformations ranging from compact to extended, wherein Pin1 exhibits different extents of interdomain contact. Previous studies have shown that weakening interdomain contact increases the isomerase activity of Pin1. Here, we propose an NMR chemical shift correlation-analysis-based method that will be general for two-domain proteins to gauge two-state populations of Pin1, and we report a linker-modified mutant of Pin1 with enhanced interdomain contact and increased isomerase activity, with the latter suggesting an uncorrelated effect of interdomain contact on isomerase activity. Thus, although bindings of different substrates in the WW domain impose opposite effects on interdomain contact, in both cases, it may promote isomerization, implying cooperativity between substrate binding in the WW domain and isomerization in the PPIase domain. |
资助项目 | National Key R&D Program of China[2016YFA051201] ; National Natural Sciences Foundation of China[21575155] ; National Natural Sciences Foundation of China[21735007] ; National Natural Sciences Foundation of China[21703283] ; K. C. Wong Educational Foundation ; Hundred Talent Program by Chinese Academy of Sciences |
WOS关键词 | SUBSTRATE RECOGNITION ; NEGATIVE REGULATION ; STRUCTURAL BASIS ; PROLYL ; ISOMERIZATION ; PATHWAYS |
WOS研究方向 | Chemistry ; Science & Technology - Other Topics ; Materials Science ; Physics |
语种 | 英语 |
出版者 | AMER CHEMICAL SOC |
WOS记录号 | WOS:000463678800017 |
资助机构 | National Key R&D Program of China ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; K. C. Wong Educational Foundation ; K. C. Wong Educational Foundation ; Hundred Talent Program by Chinese Academy of Sciences ; Hundred Talent Program by Chinese Academy of Sciences ; National Key R&D Program of China ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; K. C. Wong Educational Foundation ; K. C. Wong Educational Foundation ; Hundred Talent Program by Chinese Academy of Sciences ; Hundred Talent Program by Chinese Academy of Sciences ; National Key R&D Program of China ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; K. C. Wong Educational Foundation ; K. C. Wong Educational Foundation ; Hundred Talent Program by Chinese Academy of Sciences ; Hundred Talent Program by Chinese Academy of Sciences ; National Key R&D Program of China ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; K. C. Wong Educational Foundation ; K. C. Wong Educational Foundation ; Hundred Talent Program by Chinese Academy of Sciences ; Hundred Talent Program by Chinese Academy of Sciences |
内容类型 | 期刊论文 |
源URL | [http://ir.wipm.ac.cn/handle/112942/13792] |
专题 | 中国科学院武汉物理与数学研究所 |
通讯作者 | Zhu, Jiang; Liu, Maili |
作者单位 | 1.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 2.Chinese Acad Sci, State Key Lab Magnet Resonance & Atom Mol Phys, Key Lab Magnet Resonance Biol Syst, Natl Ctr Magnet Resonance Wuhan,Wuhan Inst Phys &, Wuhan 430071, Peoples R China |
推荐引用方式 GB/T 7714 | Yang, Yunhuang,Zhu, Jiang,Liu, Maili,et al. Uncorrelated Effect of Interdomain Contact on Pin1 Isomerase Activity Reveals Positive Catalytic Cooperativity[J]. JOURNAL OF PHYSICAL CHEMISTRY LETTERS,2019,10(6):1272-1278. |
APA | Yang, Yunhuang,Zhu, Jiang,Liu, Maili,Li, Ying,&Zhu, Wenkai.(2019).Uncorrelated Effect of Interdomain Contact on Pin1 Isomerase Activity Reveals Positive Catalytic Cooperativity.JOURNAL OF PHYSICAL CHEMISTRY LETTERS,10(6),1272-1278. |
MLA | Yang, Yunhuang,et al."Uncorrelated Effect of Interdomain Contact on Pin1 Isomerase Activity Reveals Positive Catalytic Cooperativity".JOURNAL OF PHYSICAL CHEMISTRY LETTERS 10.6(2019):1272-1278. |
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