1FMK

CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC

Summary for 1FMK

Entry DOI	10.2210/pdb1fmk/pdb
Descriptor	TYROSINE-PROTEIN KINASE SRC (2 entities in total)
Functional Keywords	src, tyrosine kinase, phosphorylation, sh2, sh3, phosphotyrosine, proto-oncogene, phosphotransferase
Biological source	Homo sapiens (human)
Cellular location	Cell membrane: P12931
Total number of polymer chains	1
Total formula weight	51709.57
Authors	Xu, W.,Harrison, S.C.,Eck, M.J. (deposition date: 1997-01-24, release date: 1997-08-20, Last modification date: 2024-10-09)
Primary citation	Xu, W.,Harrison, S.C.,Eck, M.J. Three-dimensional structure of the tyrosine kinase c-Src. Nature, 385:595-602, 1997 Cited by PubMed Abstract: The structure of a large fragment of the c-Src tyrosine kinase, comprising the regulatory and kinase domains and the carboxy-terminal tall, has been determined at 1.7 A resolution in a closed, inactive state. Interactions among domains, stabilized by binding of the phosphorylated tail to the SH2 domain, lock the molecule in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. PubMed: 9024657 DOI: 10.1038/385595a0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.5 Å)

Structure validation