6LZP
The solution structure of N-terminal elongated hSNF5 RPT1 domain
Summary for 6LZP
| Entry DOI | 10.2210/pdb6lzp/pdb |
| Descriptor | SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 (1 entity in total) |
| Functional Keywords | chromatin remodeling complex swi-snf complex, tumor suppressor, transcription, structural genomics, psi-2, protein structure initiative, structural protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 10076.29 |
| Authors | |
| 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 Cited by 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: 32244797DOI: 10.3390/ijms21072452 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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