Ovalbumin and angiotensinogen lack serpin S-R conformational change.
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ABSTRACT: 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.
SUBMITTER: Stein PE
PROVIDER: S-EPMC1133235 | biostudies-other | 1989 Aug
REPOSITORIES: biostudies-other
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