1. ¹H, ¹³C and ¹⁵N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment
- Author
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Ian B, Robertson, Isabelle, Osuch, David A, Yadin, Penny A, Handford, Sacha A, Jensen, and Christina, Redfield
- Subjects
Carbon Isotopes ,integumentary system ,Epidermal Growth Factor ,Nitrogen Isotopes ,Fibrillin-1 ,Microfibril ,Microfilament Proteins ,Molecular Sequence Data ,macromolecular substances ,Fibrillins ,Hybrid domain ,Article ,Protein Structure, Tertiary ,NMR assignment ,Humans ,Fibrillin ,Calcium ,Calcium-binding ,Amino Acid Sequence ,Nuclear Magnetic Resonance, Biomolecular ,Epidermal growth factor-like (EGF) ,Hydrogen - Abstract
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.
- Published
- 2013