Revisiting the phosphotyrosine binding pocket of Fyn SH2 domain led to the identification of novel SH2 superbinders.-Reference-Cited by-同舟云学术

Revisiting the phosphotyrosine binding pocket of Fyn SH2 domain led to the identification of novel SH2 superbinders.

Published:2020-12-31 Issue:3 Volume:30 Page:558-570
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Li Shuhao¹²³,Zou Yang²,Zhao Dongping²³,Yin Yuqing³,Song Jingyi²,He Ningning²,Liu Huadong⁴,Qian Dongmeng¹²,Li Lei²⁵,Huang Haiming³^ORCID

Affiliation:

1. College of Life Sciences Qingdao University Qingdao China

2. School of Basic Medicine Qingdao University Qingdao China

3. Department of Antibody Engineering Shanghai Asia United Antibody Medical Co., Ltd Shanghai China

4. Center for Mitochondrial Biology and Medicine, The Key Laboratory of Biomedical Information Engineering of Ministry of Education, School of Life Science and Technology Xi'an Jiaotong University Xi'an China

5. The Cancer Institute Qingdao University Qingdao China

Funder

National Natural Science Foundation of China

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4012

Reference37 articles.

1. Exploring protein fitness landscapes by directed evolution

2. The game of chess and searches in protein sequence space

3. A potent and highly specific FN3 monobody inhibitor of the Abl SH2 domain

4. Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

5. Dissection of the BCR-ABL signaling network using highly specific monobody inhibitors to the SHP2 SH2 domains

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