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Fibrillins are large extracellular glycoproteins that form the principal component of microfibrils. These perform a vital structural function in the extracellular matrix of many tissues. Fibrillins have also been implicated in mediating a number of protein-protein interactions, some of which may be significant in regulating growth factors such as transforming growth factor β. Here we present the backbone and side-chain (1)H, (13)C and (15)N assignments for a 19 kDa protein fragment derived from the N-terminus of human fibrillin-1, encompassing four domains in total. These domains include the second and third epidermal growth factor-like (EGF) domains, the first hybrid domain (hyb1), and the first calcium-binding EGF domain of fibrillin-1. This region of fibrillin-1 is of particular interest as the hyb1 domain has been suggested to play a role in microfibril assembly, as well as several other protein-protein interactions.

Original publication

DOI

10.1007/s12104-013-9481-7

Type

Journal article

Journal

Biomol NMR Assign

Publication Date

04/2014

Volume

8

Pages

189 - 194

Keywords

Amino Acid Sequence, Calcium, Carbon Isotopes, Epidermal Growth Factor, Fibrillin-1, Fibrillins, Humans, Hydrogen, Microfilament Proteins, Molecular Sequence Data, Nitrogen Isotopes, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Tertiary