Fibrillin microfibrils domains

Other recombinant studies showed that recombinant N-terminal and other regions of fibrillin-1 have a tendency to dimerise (Ashworth et al, 1999b Trask et al., 1999). An unpaired cysteine residue in the first hybrid domain, which contains nine cysteines, is predicted to be involved in covalently linking N-terminally-aligned fibrillin-1 molecules (Reinhardt et al., 2000b). N- and C-terminal halves of the fibrillin-1 molecule, and the N-terminal half of fibrillin-2, were shown to interact with high affinity in solid-phase and BIAcore binding assays (Tiedemann et al., 2001). However, N- and C-terminal fibrillin-2 polypeptides did not interact with each other. These data demonstrated that fibrillins can direcdy interact in an N- to C-terminal fashion to form homotypic fibrillin-1 or heterotypic fibrillin-1/fibrillin-2 microfibrils. 

Cardy, C. M., and Handford, P. A. (1998). Metal ion dependency of microfibrils supports a rod-like conformation for fibrillin-1 calcium-binding epidermal growth factor-like domains. J. Mol. Biol. 276, 855-860. 

Trask, T. M., Ritty, T. M., Broekelmann, T., Tisdale, C., and Mecham, R. P. (1999). N-terminal domains of fibrillin 1 and fibrillin 2 direct the formation of homodimers A possible first step in microfibril assembly. Biochem J. 340, 693-701. 

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