PDBsum entry 2y6o

Transferase

PDB id

2y6o

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Contents

			Protein chain

					263 a.a.

			Ligands

					1N1

			Waters ×302

PDB id:

2y6o

Links

Name:

Transferase

Title:

Crystal structure of epha4 kinase domain in complex with dasatinib.

Structure:

Ephrin type-a receptor 4. Chain: a. Fragment: kinase domain, residues 606-896. Synonym: epha4, tyrosine-protein kinase receptor mpk-3, tyrosine- protein kinase receptor sek-1. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.54Å

R-factor:

0.181

R-free:

0.201

Authors:

C.J.A.Farenc,P.H.N.Celie,G.Siegal

Key ref:

C.Farenc et al. (2011). Crystal structure of the EphA4 protein tyrosine kinase domain in the apo- and dasatinib-bound state. Febs Lett, 585, 3593-3599. PubMed id: 22036717

Date:

25-Jan-11

Release date:

02-Nov-11

PROCHECK

	Headers

	References

Protein chain

Q03137 (EPHA4_MOUSE) - Ephrin type-A receptor 4 from Mus musculus

Seq: Struc:

Seq: Struc:					986 a.a. 263 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.2.7.10.1 - receptor protein-tyrosine kinase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H⁺

L-tyrosyl-[protein]	+	ATP	=	O-phospho-L-tyrosyl-[protein]	+	ADP	+	H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

	Febs Lett 585:3593-3599 (2011)
PubMed id: 22036717

Crystal structure of the EphA4 protein tyrosine kinase domain in the apo- and dasatinib-bound state.
C.Farenc, P.H.Celie, C.P.Tensen, I.J.de Esch, G.Siegal.

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.