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3d7t
From Proteopedia
| 3d7t, resolution 2.90Å () | |||||||||
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| Sites: | and | ||||||||
| Ligands: | |||||||||
| Gene: | CSK (Homo sapiens), SRC (Gallus gallus) | ||||||||
| Activity: | Non-specific protein-tyrosine kinase, with EC number 2.7.10.2 | ||||||||
| Related: | 3d7u | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Structural basis for the recognition of c-Src by its inactivator Csk
The catalytic activity of the Src family of tyrosine kinases is suppressed by phosphorylation on a tyrosine residue located near the C terminus (Tyr 527 in c-Src), which is catalyzed by C-terminal Src Kinase (Csk). Given the promiscuity of most tyrosine kinases, it is remarkable that the C-terminal tails of the Src family kinases are the only known targets of Csk. We have determined the crystal structure of a complex between the kinase domains of Csk and c-Src at 2.9 A resolution, revealing that interactions between these kinases position the C-terminal tail of c-Src at the edge of the active site of Csk. Csk cannot phosphorylate substrates that lack this docking mechanism because the conventional substrate binding site used by most tyrosine kinases to recognize substrates is destabilized in Csk by a deletion in the activation loop.
Structural basis for the recognition of c-Src by its inactivator Csk., Levinson NM, Seeliger MA, Cole PA, Kuriyan J, Cell. 2008 Jul 11;134(1):124-34. PMID:18614016
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3D7T is a 2 chains structure with sequences from Gallus gallus and Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Levinson NM, Seeliger MA, Cole PA, Kuriyan J. Structural basis for the recognition of c-Src by its inactivator Csk. Cell. 2008 Jul 11;134(1):124-34. PMID:18614016 doi:10.1016/j.cell.2008.05.051
Page seeded by OCA on Wed Feb 10 16:08:38 2010
Categories: Gallus gallus | Homo sapiens | Non-specific protein-tyrosine kinase | Cole, P A. | Kuriyan, J. | Levinson, N M. | Seeliger, M A. | Alternative splicing | Atp-binding | Csk src tyrosine kinase | Cytoplasm | Kinase | Lipoprotein | Membrane | Myristate | Nucleotide-binding | Phosphoprotein | Polymorphism | Proto-oncogene | Sh2 domain | Sh3 domain | Transferase | Tyrosine-protein kinase
