Chaperones structure

Fig. 5 Chaperone structure. Ribbon diagram of FimC chaperone from the structure of the FimC FimH complex [32], p-strands in the N-terminal domain are labelled. The hydrophobic residues in the G, donor strand are shown as stick models and labelled. Also shown are the two...

Zhu, X., et al. Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272 1606-1614, 1996. 

The way in which molecular chaperones interact with polypeptides during the folding process is not completely understood. What is clear is that chaperones bind effectively to the exposed hydrophobic regions of partially folded structures. These folding intermediates are less compact than the native folded proteins. They contain large amounts of secondary and even some tertiary... 

Wearsch PA, Voglino L, Nicchitta CV (1998) Structural transitions accompanying the activation of peptide binding to the endoplasmic reticulum Hsp90 chaperone GRP94. Biochemistry 37(16) 5709-5719... 

The general types of protein-protein interactions that occur in cells include receptor-ligand, enzyme-substrate, multimeric complex formations, structural scaffolds, and chaperones. However, proteins interact with more targets than just other proteins. Protein interactions can include protein-protein or protein-peptide, protein-DNA/RNA or protein-nucleic acid, protein-glycan or protein-carbohydrate, protein-lipid or protein-membrane, and protein-small molecule or protein-ligand. It is likely that every molecule within a cell has some kind of specific interaction with a protein. 

Atxl chaperone apoprotein (without copper) shows tertiary structural differences in the loop area containing the cysteine ligand residues. Structural data for the apoprotein are deposited with PDB code 1FES.116... 

The sequence for delivery of copper ions to SOD1 passes from the copper transporter (Ctr) by an unknown pathway to the copper chaperone for SOD1 (CCS) and by a studied pathway from CCS to SOD1. The CCS protein has been studied structurally and found to be similar to other copper chaperones such as those discussed above—Atxl and Atoxl (Hahl). Copper chaperone for superoxide dismutase (CCS) differs from other copper metallochaperones in that it folds into three functionally distinct protein domains with the N-terminal end of domain I... 

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