Solution structure and backbone dynamics of the human alpha3-chain type VI collagen C-terminal Kunitz domain

Nuclear magnetic resonance spectroscopic study was utilized to describe the solution structure and backbone dynamics of the human alpha3-chain type VI collagen. Results have shown that the global fold configuration retained its form in the solution phase and assumed the same form as in the crystal phase and C5 domain core. It was indicated that the additional six residues in the N-terminal and the 12 residues in the C-terminal affected the function of the C5 domain.