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 1H, 13C and 15N 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. © 2013 The Author(s).
CITATION STYLE
Robertson, I. B., Osuch, I., Yadin, D. A., Handford, P. A., Jensen, S. A., & Redfield, C. (2014). 1H, 13C and 15N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment. Biomolecular NMR Assignments, 8(1), 189–194. https://doi.org/10.1007/s12104-013-9481-7
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