title: Complement C9 is inserted into membranes in a globular conformation.
abstract: Complement component C9 undergoes a major conformational change during its insertion into a biological membrane from a globular to an extended form. At 0 degrees C a single C9 binds but a membrane attack complex (MAC) is not formed. We show that the C9 bound at 0 degrees 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.
authors.affiliation: European Molecular Biology Laboratory, Heidelberg, FRG.
authors.forename: D
authors.initials: D
authors.lastname: Marazziti
authors.forename: J P
authors.initials: JP
authors.lastname: Luzio
authors.forename: K K
authors.initials: KK
authors.lastname: Stanley
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism*; D003186:Complement C9 / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000378:metabolism*; D011233:Precipitin Tests; D011487:Protein Conformation; D011817:Rabbits; D013816:Thermodynamics; D014357:Trypsin
chemical_list: D000911:Antibodies, Monoclonal; D003186:Complement C9; D008565:Membrane Proteins; D014357:Trypsin