3KYS

Crystal structure of human YAP and TEAD complex

Summary for 3KYS

• Entry DOI: 10.2210/pdb3kys/pdb
• Descriptor: Transcriptional enhancer factor TEF-1, 65 kDa Yes-associated protein (3 entities in total)
• Functional Keywords: immunoglobulin-like fold, activator, disease mutation, dna-binding, nucleus, phosphoprotein, transcription, transcription regulation, transcription-protein binding complex, transcription/protein binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 77682.22

Authors

Li, Z.,Zhao, B.,Wang, P.,Chen, F.,Dong, Z.,Yang, H.,Guan, K.L.,Xu, Y. (deposition date: 2009-12-07, release date: 2010-02-23, Last modification date: 2020-10-07)

Primary citation

Li, Z.,Zhao, B.,Wang, P.,Chen, F.,Dong, Z.,Yang, H.,Guan, K.L.,Xu, Y.
Structural insights into the YAP and TEAD complex
Genes Dev., 24:235-240, 2010

PubMed Abstract: The Yes-associated protein (YAP) transcriptional coactivator is a key regulator of organ size and a candidate human oncogene inhibited by the Hippo tumor suppressor pathway. The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression. Here we report the three-dimensional structure of the YAP (residues 50-171)-TEAD1 (residues 194-411) complex, in which YAP wraps around the globular structure of TEAD1 and forms extensive interactions via three highly conserved interfaces. Interface 3, including YAP residues 86-100, is most critical for complex formation. Our study reveals the biochemical nature of the YAP-TEAD interaction, and provides a basis for pharmacological intervention of YAP-TEAD hyperactivation in human diseases.

PubMed: 20123905
DOI: 10.1101/gad.1865810

Experimental method

X-RAY DIFFRACTION (2.8 Å)