6XYX

Crystal structure of the BCL6 BTB domain in complex with the NCoR1 BBD corepressor peptide

6XYX の概要

• エントリーDOI: 10.2210/pdb6xyx/pdb
• 分子名称: B-cell lymphoma 6 protein, Nuclear receptor corepressor 1, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: bcl6, ncor1., transcription
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 32990.19

構造登録者

Zacharchenko, T.,Wright, S.C. (登録日: 2020-01-31, 公開日: 2020-12-02, 最終更新日: 2024-01-24)

主引用文献

Zacharchenko, T.,Wright, S.
Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone.
Iucrj, 8:154-160, 2021

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: 33708392
DOI: 10.1107/S2052252520015754

実験手法

X-RAY DIFFRACTION (1.44 Å)