Article info Vol. 6  No. 3   pp.  56 ~ 59
Title Crystallization and preliminary diffraction analysis of human TEAD1, a transcriptional enhancer factor that controls the Hippo signaling pathway
Authors Yeajin Mo1,2†, Hye Seon Lee1,2†, Chang Hoon Lee3, Hwan Jung Lim3, Seong Jun Park3, Ho-Chul Shin1, Seung Jun Kim1* and Bonsu Ku1*
Institutions 1Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Republic of Korea, 2Department of Biology, Chungnam National University, Daejeon 34134, Republic of Korea, 3Center for Information-Based Drug Research, Korea Research Institute of Chemical Technology, Daejeon 34114, Republic of Korea *Correspondence: ksj@kribb.re.kr, bku@kribb.re.kr †These authors equally contributed to this work.
Abstract Transcriptional enhancer activation domain (TEAD) proteins are transcription factors that promote the expression of genes involved in organogenesis, embryonic development, and tumorigenesis. TEAD functions downstream of the Hippo signaling pathway as one of the pivotal regulators that controls cell viability and proliferation, tissue growth, and organ size, by interacting with yes-associated protein (YAP) via its C-terminal YAP-binding domain (YBD). As YAP is a wellknown oncoprotein and its interaction with TEAD has been shown to be critical for the function of YAP, TEAD proteins are emerging as a potential therapeutic target for cancer. In this study, the YBD of the TEAD1 protein was produced from an Escherichia coli expression system, purified using a Ni-NTA affinity chromatography, HiTrap Q anion exchange chromatography, and size exclusion chromatography, and then successfully crystallized. X-ray diffraction data were collected to the resolution of 1.70 Å. Preliminary diffraction analysis revealed that the TEAD1 YBD crystals belong to the space group P212121 with unit cell parameters of a = 36.5 Å, b = 89.4 Å, c = 135.6 Å, and that two TEAD1 YBD molecules are contained in the asymmetric unit with a solvent content of 45.2%.