Crystal structure of the SH3 domain of human Lyn non-receptor tyrosine kinase.

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Berndt S, Gurevich VV, Iverson TM

Crystal structure of the SH3 domain of human Lyn non-receptor tyrosine kinase.

PLoS One. 2019 Apr 10;14(4):e0215140. doi: 10.1371/journal.pone.0215140. eCollection 2019.

PubMed ID

30969999 [ View in PubMed

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Abstract

Lyn kinase (Lck/Yes related novel protein tyrosine kinase) belongs to the family of Src-related non-receptor tyrosine kinases. Consistent with physiological roles in cell growth and proliferation, aberrant function of Lyn is associated with various forms of cancer, including leukemia, breast cancer and melanoma. Here, we determine a 1.3 A resolution crystal structure of the polyproline-binding SH3 regulatory domain of human Lyn kinase, which adopts a five-stranded beta-barrel fold. Mapping of cancer-associated point mutations onto this structure reveals that these amino acid substitutions are distributed throughout the SH3 domain and may affect Lyn kinase function distinctly.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Bosutinib	Tyrosine-protein kinase Lyn	Protein	Humans	Yes	Inhibitor	Details