2Y6O

Crystal structure of EphA4 kinase domain in complex with Dasatinib.

Summary for 2Y6O

• Entry DOI: 10.2210/pdb2y6o/pdb
• Related: 1B0X 2XYU 2Y6M
• Descriptor: EPHRIN TYPE-A RECEPTOR 4, N-(2-CHLORO-6-METHYLPHENYL)-2-({6-[4-(2-HYDROXYETHYL)PIPERAZIN-1-YL]-2-METHYLPYRIMIDIN-4-YL}AMINO)-1,3-THIAZOLE-5-CARBOXAMIDE (3 entities in total)
• Functional Keywords: signalling protein, transferase
• Biological source: MUS MUSCULUS (HOUSE MOUSE)
• Cellular location: Cell membrane; Single-pass type I membrane protein: Q03137
• Total number of polymer chains: 1
• Total formula weight: 33419.08

Authors

Farenc, C.J.A.,Celie, P.H.N.,Siegal, G. (deposition date: 2011-01-25, release date: 2011-11-02, Last modification date: 2023-12-20)

Primary citation

Farenc, C.J.A.,Hameetman, L.,Zoutman, W.,Tensen, C.P.,Siegal, G.
Crystal Structure of the Epha4 Protein Tyrosine Kinase Domain in the Apo- and Dasatinib-Bound State.
FEBS Lett., 585:3593-, 2011

PubMed Abstract: The Eph family of receptor tyrosine kinases regulates diverse cellular processes while the over-expression of a member of this family, EphA4, has been reported in a variety of malignant carcinomas. To gain insight into molecular mechanisms and to facilitate structure-based inhibitor design, we solved the crystal structure of the native EphA4 kinase domain in both the apo and dasatinib bound forms. Analysis of the two structures provides insight into structural features of inhibitor binding and revealed a hydrophobic back-pocket in the ATP- binding site of EphA4 which was previously unidentified. The structures suggest a route towards development of novel and specific inhibitors.

PubMed: 22036717
DOI: 10.1016/J.FEBSLET.2011.10.028

Experimental method

X-RAY DIFFRACTION (1.543 Å)