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Complement C9 is inserted into membranes in a globular conformation
Author(s) -
Marazziti Daniela,
Luzio J.Paul,
Stanley Keith K.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80159-0
Subject(s) - globular cluster , complement (music) , membrane , chemistry , complement system , biophysics , crystallography , biochemistry , biology , physics , genetics , antibody , gene , stars , complementation , phenotype , astronomy
Complement component C9 undergoes a major conformational change during its insertion into a biological membrane from a globular to an extended form. At 0°C a single C9 binds but a membrane attack complex (MAC) is not formed. We show that the C9 bound at 0°C is accessible to the intracellular space and sensitive to trypsin digestion, suggesting that C9 inserts in its globular state and requires an elevated temperature in order to change conformation. Complement; C9; Membrane assembly; Cytotoxicity