6KZ7

The crystal structure of BAF155 SWIRM domain and N-terminal elongated hSNF5 RPT1 domain complex: Chromatin remodeling complex

Summary for 6KZ7

• Entry DOI: 10.2210/pdb6kz7/pdb
• Descriptor: SWI/SNF complex subunit SMARCC1, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 (3 entities in total)
• Functional Keywords: swi-snf complex, tumor suppressor, transcription
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 41058.52

Authors

Lee, W.,Han, J.,Kim, I.,Park, J.H.,Joo, K.,Lee, J.,Suh, J.Y. (deposition date: 2019-09-23, release date: 2020-07-08, Last modification date: 2024-03-27)

Primary citation

Han, J.,Kim, I.,Park, J.H.,Yun, J.H.,Joo, K.,Kim, T.,Park, G.Y.,Ryu, K.S.,Ko, Y.J.,Mizutani, K.,Park, S.Y.,Seong, R.H.,Lee, J.,Suh, J.Y.,Lee, W.
A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction.
Int J Mol Sci, 21:-, 2020

PubMed Abstract: Human SNF5 and BAF155 constitute the core subunit of multi-protein SWI/SNF chromatin-remodeling complexes that are required for ATP-dependent nucleosome mobility and transcriptional control. Human SNF5 (hSNF5) utilizes its repeat 1 (RPT1) domain to associate with the SWIRM domain of BAF155. Here, we employed X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and various biophysical methods in order to investigate the detailed binding mechanism between hSNF5 and BAF155. Multi-angle light scattering data clearly indicate that hSNF5 and BAF155 are both monomeric in solution and they form a heterodimer. NMR data and crystal structure of the hSNF5/BAF155 complex further reveal a unique binding interface, which involves a coil-to-helix transition upon protein binding. The newly formed α helix of hSNF5 interacts with the β2-α1 loop of hSNF5 via hydrogen bonds and it also displays a hydrophobic interaction with BAF155. Therefore, the -terminal region of hSNF5 plays an important role in tumorigenesis and our data will provide a structural clue for the pathogenesis of Rhabdoid tumors and malignant melanomas that originate from mutations in the -terminal loop region of hSNF5.

PubMed: 32244797
DOI: 10.3390/ijms21072452

Experimental method

X-RAY DIFFRACTION (2.28 Å)