Entropic allostery dominates the phosphorylation-dependent regulation of Syk tyrosine kinase release from immunoreceptor tyrosine-based activation motifs.

Feng, Chao; Roy, Amitava; Post, Carol Beth

Feng, Chao; Roy, Amitava; Post, Carol Beth.

Affiliation

Feng C; Department of Medicinal Chemistry and Molecular Pharmacology, Markey Center for Structural Biology, and Purdue Center for Cancer Research, Purdue University, West Lafayette, Indiana, 47907.
Roy A; Bioinformatics and Computational Biosciences Branch, Rocky Mountain Laboratories, NIAID, National Institutes of Health, Hamilton, Montana, 59840.
Post CB; Department of Medicinal Chemistry and Molecular Pharmacology, Markey Center for Structural Biology, and Purdue Center for Cancer Research, Purdue University, West Lafayette, Indiana, 47907.

Protein Sci ; 27(10): 1780-1796, 2018 10.

Article in En | MEDLINE | ID: mdl-30051939

Subject(s)

Entropy; Syk Kinase/metabolism; Humans; Immunoreceptor Tyrosine-Based Activation Motif; Models, Molecular; Phosphorylation; Syk Kinase/chemistry

Key words

NMR chemical shift difference analysis; doubly phosphorylated immunoreceptor tyrosine-based activation motif (dp-ITAM); entropic allostery; isothermal titration calorimetry model and data analysis; multi-domain ensemble thermodynamics; multistate equilibrium with isomerization; regulation of protein-protein interaction; spleen tyrosine kinase (Syk); tandem SH2 domain (tSH2); tyrosine phosphorylation allostery

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Entropy / Syk Kinase Limits: Humans Language: En Journal: Protein Sci Journal subject: BIOQUIMICA Year: 2018 Type: Article

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