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A new zinc binding fold underlines the versatility of zinc binding modules in protein evolution
journal contribution
posted on 2023-05-17, 02:59 authored by Sharpe, BK, Matthews, JM, Kwan, AH, Newton, A, David GellDavid Gell, Crossley, M, Mackay, JPMany different zinc binding modules have been identified. Their abundance and variety suggests that the formation of zinc binding folds might be relatively common. We have determined the structure of CH11, a 27-residue peptide derived from the first cysteine/histidine-rich region (CH1) of CREB binding protein (CBP). This peptide forms a highly ordered zinc-dependent fold that is distinct from known folds. The structure differs from a subsequently determined structure of a larger region from the CH3 region of CBP, and the CH11 fold probably represents a nonphysiologically active form. Despite this, the fold is thermostable and tolerant to both multiple alanine mutations and changes in the zinc-ligand spacing. Our data support the idea that zinc binding domains may arise frequently. Additionally, such structures may prove useful as scaffolds for protein design, given their stability and robustness.
History
Publication title
StructureVolume
10Issue
5Pagination
639-648ISSN
0969-2126Department/School
Menzies Institute for Medical ResearchPublisher
Cell PressPlace of publication
1100 Massachusetts Ave, Cambridge, USA, Ma, 02138Repository Status
- Restricted