Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders

Article Abstract:

The covalently linked pair of calcium-binding epidermal growth factor-like (cbEGF) domains exhibits an extended rod-like conformation. A novel structure for fibrillin-1 cbEGF which is defective in the Marfan syndrome was proposed. The 32nd and 33rd cbEGF domains from the human fibrillin-1 are fixed in an extended conformation. Calcium ligation and hydrophobic packing interactions stabilizes the domain interface. The model provides possible explanations for the disease-causing mutations such as Marfan syndrome and hypercholesterolemia.

Physiological aspects, Epidermal growth factor, Epidermal growth factors, Marfan syndrome

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Acetlycholinesterase inhibition by fasciculin: crystal structure of the complex

Article Abstract:

The binding of the snake toxin fasciculin to acetylcholinesterase (AChE) produces structural changes in the enzyme, which reduce its catalytic activity. A study of the X-ray structure of the complex between mouse AChE and fasciculin indicates a synergistic three-point binding. Loop II of fasciculin has a group of hydrophobic residues that interact with the anionic region of the enzyme and sterically hinder substrate binding. Loop I plays a role in maintaining the coupling of loop II to the enzyme.

Research, Observations, Acetylcholinesterase, Enzyme inhibitors

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Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell

Article Abstract:

The X-ray crystallographic structure of the flavoenzyme Ero1p, which produces disulfide bonds for oxidative protein folding in the endoplasmic reticulum, is examined. Both Ero1p and Erv2p display essential dicysteine motifs on mobile polypeptide segments, suggesting that shuttling electrons to a rigid active site using a flexible strand is a fundamental feature of disulphide-generating flavoenzymes.

Enzymes, Other Basic Organic Chemical Manufacturing, Atomic properties

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