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 well-known 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 P2 1 2 1 2 1 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%.
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RESULTS AND DISCUSSION
METHODS