[HTML][HTML] The Cys6 intermolecular disulfide bond and the collagen-like region of rat SP-A play critical roles in interactions with alveolar type II cells and surfactant lipids
FX McCormack, S Pattanajitvilai, J Stewart… - Journal of Biological …, 1997 - ASBMB
Rat pulmonary surfactant protein A is an oligomer of 18 polypeptide chains which are
associated by triple helix formation in the collagen-like domain and interchain disulfide
bridges at the NH 2 terminus. The roles of the intermolecular bond at Cys 6 and the collagen-
like domain (Gly 8-Pro 80) in the interactions of SP-A with phospholipids and alveolar type II
cells were investigated using mutant forms of the protein. Wild type SP-A (SP-A hyp), SP-A
with the substitution Cys 6→ Ser to prevent disulfide formation (SP-A hyp, C6S), and SP-A …
associated by triple helix formation in the collagen-like domain and interchain disulfide
bridges at the NH 2 terminus. The roles of the intermolecular bond at Cys 6 and the collagen-
like domain (Gly 8-Pro 80) in the interactions of SP-A with phospholipids and alveolar type II
cells were investigated using mutant forms of the protein. Wild type SP-A (SP-A hyp), SP-A
with the substitution Cys 6→ Ser to prevent disulfide formation (SP-A hyp, C6S), and SP-A …
