Ovalbumin and angiotensinogen lack serpin S-R conformational change.
Cleavage of ovalbumin and angiotensinogen at sites homologous to the reactive centre loop of alpha 1-antitrypsin is not accompanied by the increase in heat-stability associated with the transition from the native stressed (S) structure to a cleaved relaxed (R) form that is typical of other serpins. Failure to undergo the S-R change in ovalbumin is not due to phosphorylation of Ser-344 near the sites of cleavage on the loop. The suggested explanation is the unique presence of bulky side chains at the P10-P12 site in ovalbumin and angiotensinogen.
Stein
P E
PE
Department of Haematology, University of Cambridge, U.K.
Tewkesbury
D A
DA
Carrell
R W
RW
D000595:Amino Acid Sequence; D000808:Angiotensinogen / Q000032:analysis*; D006358:Hot Temperature; D006801:Humans; D008969:Molecular Sequence Data; D010047:Ovalbumin / Q000032:analysis*; D011487:Protein Conformation; D015842:Serine Proteinase Inhibitors
D015842:Serine Proteinase Inhibitors; D000808:Angiotensinogen; D010047:Ovalbumin