Unique allosteric mechanism regulating protein-protein interaction through phosphorylation: a case study of the conformational changes in the Syk tandem SH2 protein

被引：0

作者：

Hua, Duy P. ^{[1
]}

Post, Carol Beth ^{[1
]}

机构：

[1] Purdue Univ, Dept Med Chem & Mol Pharmacol, W Lafayette, IN 47907 USA

来源：

PROTEIN SCIENCE | 2016年 / 25卷

关键词：

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

引用

页码：37 / 37

页数：1

共 19 条

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[13] The human immunodeficiency virus type 1 NEF protein binds the Src-related tyrosine kinase Lck SH2 domain through a novel phosphotyrosine independent mechanism
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[16] Phosphotyrosine-independent binding of a 62-kDa protein to the src hornology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region
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[17] Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56(lck) and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region
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[18] Computational analysis of protein stability and allosteric interaction networks in distinct conformational forms of the SARS-CoV-2 spike D614G mutant: reconciling functional mechanisms through allosteric model of spike regulation
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[19] Pre-S2 mutant surface antigen of hepatitis B virus induces retinoblastoma hyper-phosphorylation through interaction with JAB1 protein in endoplasmic reticulum: a novel mechanism for HBV-induced hepatocellular carcinoma
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