6Y17
Crystal structure of an NCoR1BBD2-BCL6BTB chimera in complex with nebulinSH3-NCoR1BBD1
Summary for 6Y17
| Entry DOI | 10.2210/pdb6y17/pdb |
| Descriptor | Nuclear receptor corepressor 1,B-cell lymphoma 6 protein, Nebulin,Nuclear receptor corepressor 1, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | bcl6, ncor1., transcription |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 48956.96 |
| Authors | Zacharchenko, T.,Wright, S.C. (deposition date: 2020-02-11, release date: 2020-12-02, Last modification date: 2024-01-24) |
| Primary citation | Zacharchenko, T.,Wright, S. Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone. Iucrj, 8:154-160, 2021 Cited by PubMed Abstract: The production of diffraction-quality protein crystals is challenging and often requires bespoke, time-consuming and expensive strategies. A system has been developed in which the BCL6 BTB domain acts as a crystallization chaperone and promiscuous assembly block that may form the basis for affinity-capture crystallography. The protein of interest is expressed with a C-terminal tag that interacts with the BTB domain, and co-crystallization leads to its incorporation within a BTB-domain lattice. This strategy was used to solve the structure of the SH3 domain of human nebulin, a structure previously solved by NMR, at 1.56 Å resolution. This approach is simple and effective, requiring only routine protein complexation and crystallization screening, and should be applicable to a range of proteins. PubMed: 33708392DOI: 10.1107/S2052252520015754 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
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