7F09

Crystal structure of the HLH-Lz domain of human TFE3

Summary for 7F09

• Entry DOI: 10.2210/pdb7f09/pdb
• Descriptor: Transcription factor E3, 1,2-ETHANEDIOL, ZINC ION, ... (4 entities in total)
• Functional Keywords: transcription factor e3, hlh-lz domain, transcription
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 4
• Total formula weight: 35268.12

Authors

Yang, G.,Li, P.,Liu, Z.,Wu, S.,Zhuang, C.,Qiao, H.,Fang, P.,Wang, J. (deposition date: 2021-06-03, release date: 2021-07-21, Last modification date: 2023-11-29)

Primary citation

Yang, G.,Li, P.,Liu, Z.,Wu, S.,Zhuang, C.,Qiao, H.,Zheng, L.,Fang, P.,Lei, C.,Wang, J.
Structural basis for the dimerization mechanism of human transcription factor E3.
Biochem.Biophys.Res.Commun., 569:41-46, 2021

PubMed Abstract: The transcription factor for immunoglobulin heavy-chain enhancer 3 (TFE3) is a member of the microphthalmia (MiT/TFE) transcription factor family. Dysregulation of TFE3 due to chromosomal abnormalities is associated with a subset of human renal cell carcinoma. Little structural information of this key transcription factor has been reported. In this study, we determined the crystal structure of the helix-loop-helix leucine zipper (HLH-Lz) domain of human TFE3 to a resolution of 2.6 Å. The HLH-Lz domain is critical for the dimerization and function of TFE3. Our structure showed that the conserved HLH region formed a four-helix bundle structure with a predominantly hydrophobic core, and the leucine zipper region contributed to the function of TFE3 by promoting dimer interaction and providing partner selectivity. Together, our results elucidated the dimerization mechanism of this important transcription factor, providing the structural basis for the development of inhibiting strategies for treating TFE3 dysregulated diseases.

PubMed: 34225079
DOI: 10.1016/j.bbrc.2021.06.091

Experimental method

X-RAY DIFFRACTION (2.6 Å)