pISSN 2288-6982
eISSN 2288-7105




BioDesign 2021; 9(3): 55-58

Published online September 30, 2021

© Korean Society for Structural Biology

Purification, crystallization and X-ray crystallographic analysis of RPTPH

Myeongbin Kim and Seong Eon Ryu*

Department of Bioengineering, College of Engineering, Hanyang University, Seoul 04763, Republic of Korea

Correspondence to: *

Received: August 17, 2021; Revised: September 14, 2021; Accepted: September 14, 2021


Receptor-type protein tyrosine phosphatases (RPTPs) belong to the protein tyrosine phosphatase (PTP) family and play a critical role in cell signaling. RPTPH, a type of RPTP, consists of long extracellular domains, a transmembrane domain, and a single intracellular domain with phosphatase activity. RPTPH is involved in phosphorylation of target proteins involved in the AKT signaling pathway and regulates T-cell function and cell apoptosis. The protein is also implicated in progression of colorectal and lung cancers. Despite the importance of RPTPH in tumor-related cell signaling and therapeutic drug development, the structure of this enzyme has not yet been determined. We overexpressed, purified, and crystallized the catalytic domain of RPTPH. The RPTPH crystal diffracted at a resolution of 1.56 Å. It belonged to the space group P32 with unit cell parameters a = b = 56.46 Å, c = 80.45 Å, α = β = 90°, and γ = 120°.