Substrate binding to Src: A new perspective on tyrosine kinase substrate recognition from NMR and molecular dynamics.

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作者： Mehul K,Joshi ^[1] ; Robert A,Burton ^[1] ; Heng,Wu ^[2] ; Andrew M,Lipchik ^[1] ; Barbara P,Craddock ^[1] ; Huaping,Mo ^[3] ; Laurie L,Parker ^[4] ; W Todd,Miller ^[1] ; Carol Beth,Post ^[3]

作者单位： Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, Indiana. ^[1] Ancestry, Lehi, Utah. ^[2] Department of Physiology and Biophysics, School of Medicine, Stony Brook University, Stony Brook, New York. ^[3] Purdue Interdepartmental NMR Facility PINMRF, Purdue University, West Lafayette, Indiana. ^[4] Department of Veterans Affairs Medical Center, Northport, New York. ^[5]

关键词 chemical shift perturbation clustering conformational ensembles ensemble averaging NMR restraints kinase-substrate molecular recognition multiple ligand-binding modes paramagnetic relaxation enhancement substrate recognition

主题词人类(Humans);分子动力学模拟(Molecular Dynamics Simulation);核磁共振, 生物分子(Nuclear Magnetic Resonance, Biomolecular);肽类(Peptides);蛋白质结合(Protein Binding);底物特异性(Substrate Specificity);src族激酶类(src-Family Kinases)

DOI 10.1002/pro.3777

PMID 31697410

发布时间 2022-04-14

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