1LIQ

Non-native Solution Structure of a fragment of the CH1 domain of CBP

Summary for 1LIQ

• Entry DOI: 10.2210/pdb1liq/pdb
• NMR Information: BMRB: 5369
• Descriptor: CREB Binding Protein, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger, protein design, protein binding
• Cellular location: Cytoplasm: Q92793
• Total number of polymer chains: 1
• Total formula weight: 3138.07

Authors

Sharpe, B.K.,Matthews, J.M.,Kwan, A.H.Y.,Newton, A.,Gell, D.A.,Crossley, M.,Mackay, J.P. (deposition date: 2002-04-18, release date: 2002-05-29, Last modification date: 2024-05-29)

Primary citation

Sharpe, B.K.,Matthews, J.M.,Kwan, A.H.Y.,Newton, A.,Gell, D.A.,Crossley, M.,Mackay, J.P.
A New Zinc Binding Fold Underlines the Versatility of Zinc Binding Modules in Protein Evolution
Structure, 10:639-648, 2002

PubMed Abstract: 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 CH1(1), 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 CH1(1) 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.

PubMed: 12015147
DOI: 10.1016/S0969-2126(02)00757-8

Experimental method

SOLUTION NMR