Crystal structure of the kinase domain of human protein tyrosine kinase 6 (PTK6) at 2.33 Å resolution

Thakur, Manish Kumar and Amit Kumar and Swarnakumari, B. and Swaminathan, Srinivasan and Tyagi, Rajiv and Gosu, Ramachandraiah (2016) Crystal structure of the kinase domain of human protein tyrosine kinase 6 (PTK6) at 2.33 Å resolution. Biochemical and Biophysical Research Communications, 478 (2). 637 - 642.

Full text not available from this repository. (Request a copy)
Official URL: https://doi.org/10.1016/j.bbrc.2016.07.121

Abstract

Human Protein tyrosine kinase 6 (PTK6) (EC:2.7.10.2), also known as the breast tumor kinase (BRK), is an intracellular non-receptor Src-related tyrosine kinase expressed in a majority of human breast tumors and breast cancer cell lines, but its expression is low or completely absent in normal mammary glands. In the recent past, several studies have suggested that PTK6 is a potential therapeutic target in cancer. To understand its structural and functional properties, the PTK6 kinase domain (PTK6-KD) gene was cloned, overexpressed in a baculo-insect cell system, purified and crystallized at room temperature. X-ray diffraction data to 2.33 Å resolution was collected on a single PTK6-KD crystal, which belonged to the triclinic space group P1. The Matthews coefficient calculation suggested the presence of four protein molecules per asymmetric unit, with a solvent content of ∼50.The structure has been solved by molecular replacement and crystal structure data submitted to the protein data bank under the accession number 5D7V. This is the first report of apo PTK6-KD structure crystallized in DFG-in and αC-helix-out conformation.

Item Type: Article
Uncontrolled Keywords: PTK6, BRK, Non-receptor tyrosine kinase, Kinase domain, X-ray crystal structure, Cancer
Subjects: C Chemical Science > Biochemistry
Divisions: Department of > Biochemistry
Depositing User: Manjula P Library Assistant
Date Deposited: 19 Jun 2019 05:04
Last Modified: 05 Jul 2022 05:59
URI: http://eprints.uni-mysore.ac.in/id/eprint/3379

Actions (login required)

View Item View Item