Many 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.

Item Type:	Refereed Article
Research Division:	Biological Sciences
Research Group:	Biochemistry and Cell Biology
Research Field:	Structural Biology (incl. Macromolecular Modelling)
Objective Division:	Expanding Knowledge
Objective Group:	Expanding Knowledge
Objective Field:	Expanding Knowledge in the Biological Sciences
Author:	Gell, DA (Dr David Gell)
ID Code:	64560
Year Published:	2002
Web of Science® Times Cited:	18
Deposited By:	Menzies Institute for Medical Research
Deposited On:	2010-08-12
Last Modified:	2011-08-02
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