6NMW

Crystal structure of the human Lyn SH3 domain

Summary for 6NMW

Entry DOI	10.2210/pdb6nmw/pdb
Descriptor	Tyrosine-protein kinase Lyn (2 entities in total)
Functional Keywords	lyn kinase, src family kinase, non-receptor tyrosine kinase, sh3 domain, oncoprotein
Biological source	Homo sapiens (Human)
Total number of polymer chains	1
Total formula weight	8075.15
Authors	Berndt, S.,Gurevich, V.V.,Iverson, T.M. (deposition date: 2019-01-12, release date: 2019-04-17, Last modification date: 2023-10-11)
Primary citation	Berndt, S.,Gurevich, V.V.,Iverson, T.M. Crystal structure of the SH3 domain of human Lyn non-receptor tyrosine kinase. PLoS ONE, 14:e0215140-e0215140, 2019 Cited by PubMed 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 Å resolution crystal structure of the polyproline-binding SH3 regulatory domain of human Lyn kinase, which adopts a five-stranded β-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. PubMed: 30969999 DOI: 10.1371/journal.pone.0215140 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.199 Å)

Structure validation