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Solution structure of SHIP2 SH2 domain and its interaction with a phosphotyrosine peptide from c-MET

文献类型：期刊论文

作者Yang, Yunhuang4; Zhu, Jiang4; Liu, Maili4; Kennedy, Michael A.1; Ramelot, Theresa A.1; Xu, Henghao2; Zhang, Kunxiao2; Nie, Yao3,4; Wang, Zi3,4
刊名ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
出版日期2018-10-15
卷号656页码:31-37
ISSN号0003-9861
关键词INPPLI HGFR SH2 domain Solution NMR structure Tyrosine phosphorylation
DOI10.1016/j.abb.2018.08.012
英文摘要SH2 domain-containing inositol 5-phosphatase 2 (SHIP2) binds with the Y1356-phosphorylated hepatocyte growth factor (HGF) receptor, c-MET, through its SH2 domain, which is essential for the role of SHIP2 in HGFinduced cell scattering and cell spreading. Previously, the experimental structure of the SH2 domain from SHIP2 (SHIP2-SH2) had not been reported, and its interaction with the Y1356-phosphorylated c-MET had not been investigated from a structural point of view. In this study, the solution structure of SHIP2-SH2 was determined by NMR spectroscopy, where it was found to adopt a typical SH2-domain fold that contains a positively-charged pocket for binding to phosphotyrosine (pY). The interaction between SHIP2-SH2 and a pY-containing peptide from c-MET (Y1356 phosphorylated) was investigated through NMR titration. The results showed that the binding affinity of SHIP2-SH2 with the phosphopeptide is at low micromolar level, and the binding interface consists of the positively-charged pocket and its surrounding regions. Furthermore, R28, S49 and R70 were identified as key residues for the binding and may directly interact with the pY. Taken together, these findings provide structural insights into the binding of SHIP2-SH2 with the Y1356-phosphorylated c-MET, and lay a foundation for further studies of the interactions between SHIP2-SH2 and its various binding partners.
WOS关键词LIPID PHOSPHATASE SHIP2 ; INOSITOL 5-PHOSPHATASE SHIP2 ; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE ; POLYPHOSPHATE 5-PHOSPHATASES ; SIGNAL-TRANSDUCTION ; PROTEIN STRUCTURES ; COMPLEX ; ACTIVATION ; RATIONALE ; MEMBRANE
资助项目National Key R&D Program of China[2016YFA051201] ; National Natural Sciences Foundation of China[21575155] ; Hundred Talent Program by Chinese Academy of Sciences ; Open-end Funds of Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening[HY201701] ; National Institute of General Medical Sciences of USA[U54-GM094597]
WOS研究方向Biochemistry & Molecular Biology ; Biophysics
语种英语
出版者ELSEVIER SCIENCE INC
WOS记录号WOS:000448231200003
资助机构National Key R&D Program of China ; National Natural Sciences Foundation of China ; Hundred Talent Program by Chinese Academy of Sciences ; Open-end Funds of Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening ; National Institute of General Medical Sciences of USA ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; Hundred Talent Program by Chinese Academy of Sciences ; Open-end Funds of Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening ; National Institute of General Medical Sciences of USA ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; Hundred Talent Program by Chinese Academy of Sciences ; Open-end Funds of Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening ; National Institute of General Medical Sciences of USA ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; Hundred Talent Program by Chinese Academy of Sciences ; Open-end Funds of Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening ; National Institute of General Medical Sciences of USA
源URL[http://ir.wipm.ac.cn/handle/112942/13205]  
专题中国科学院武汉物理与数学研究所
通讯作者Yang, Yunhuang; Zhu, Jiang
作者单位1.Miami Univ, Dept Chem & Biochem, Northeast Struct Genom Consortium, Oxford, OH 45056 USA
2.Huaihai Inst Technol, Jiangsu Key Lab Marine Pharmaceut Compound Screen, Lianyungang 222005, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
4.Chinese Acad Sci, Wuhan Inst Phys & Math, Wuhan Ctr Magnet Resonance, State Key Lab Magnet Resonance & Atom Mol Phys, Wuhan 430071, Hubei, Peoples R China
推荐引用方式
GB/T 7714		 Yang, Yunhuang,Zhu, Jiang,Liu, Maili,et al. Solution structure of SHIP2 SH2 domain and its interaction with a phosphotyrosine peptide from c-MET[J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS,2018,656:31-37.
APA Yang, Yunhuang.,Zhu, Jiang.,Liu, Maili.,Kennedy, Michael A..,Ramelot, Theresa A..,...&Wang, Zi.(2018).Solution structure of SHIP2 SH2 domain and its interaction with a phosphotyrosine peptide from c-MET.ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS,656,31-37.
MLA Yang, Yunhuang,et al."Solution structure of SHIP2 SH2 domain and its interaction with a phosphotyrosine peptide from c-MET".ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 656(2018):31-37.

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来源：武汉物理与数学研究所

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