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 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.
Highlights
Fibrillins are large extracellular glycoproteins that form the principal component of microfibrils
Fibrillins have 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 b
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
Summary
Fibrillins assemble into oligomeric microfibrils, 10–12 nm in diameter, with a ‘‘beads on a string’’ appearance when. The interaction with LTBPs is of particular interest, as it may sequester TGFb to microfibrils, and could play a role in disease progression in Marfan syndrome (MFS), where fibrillin haploinsufficiency has been associated with over-activation of TGFb (Neptune et al 2003). We present backbone and side-chain assignments for the EGF2-EGF3-hyb1-cbEGF1 domains of human fibrillin-1 (FBN1e2cb1) (Fig. 1a), derived from a protein fragment of 177 amino acids, from Ser 113 to Glu 287. These assignments will be used to investigate the structure and dynamics of this four-domain fibrillin-1 fragment, and. Determine potential binding sites for LTBPs and other molecules
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