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• W2029788082 startingPage "1065" @default.
• W2029788082 abstract "Calcium binding (cb) epidermal growth factor-like (EGF) domains are found in a wide variety of extracellular proteins with diverse functions. In several proteins, including the fibrillins (1 and 2), the low-density lipoprotein receptor, the Notch receptor and related molecules, these domains are organised as multiple tandem repeats. The functional importance of calcium-binding by EGF domains has been underscored by the identification of missense mutations associated with defective calcium-binding, which have been linked to human diseases. Here, we present (15)N backbone relaxation data for a pair of cbEGF domains from fibrillin-1, the defective protein in the Marfan syndrome. The data were best fit using a symmetric top model, confirming the extended conformation of the cbEGF domain pair. Our data demonstrate that calcium plays a key role in stabilising the rigidity of the domain pair on the pico- to millisecond time-scale. Strikingly, the most dynamically stable region of the construct is centred about the domain interface. These results provide important insight into the properties of intact fibrillin-1, the consequences of Marfan syndrome causing mutations, and the ultrastructure of fibrillins and other extracellular matrix proteins." @default.
• W2029788082 created "2016-06-24" @default.
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• W2029788082 date "2000-03-01" @default.
• W2029788082 modified "2023-10-03" @default.
• W2029788082 title "Backbone dynamics of a cbEGF domain pair in the presence of calcium 1 1Edited by M. Summers" @default.
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• W2029788082 doi "https://doi.org/10.1006/jmbi.1999.3513" @default.
• W2029788082 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10686104" @default.
• W2029788082 hasPublicationYear "2000" @default.
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