Dataset Information

The conformational change of the protease inhibitor α₂-macroglobulin is triggered by the retraction of the cleaved bait region from a central channel.

ABSTRACT: The protease inhibitor α₂-macroglobulin (A2M) is a member of the ancient α₂-macroglobulin superfamily (A2MF), which also includes structurally related proteins, such as complement factor C3. A2M and other A2MF proteins undergo an extensive conformational change upon cleavage of their bait region by proteases. However, the mechanism whereby cleavage triggers the change has not yet been determined. We have previously shown that A2M remains functional after completely replacing its bait region with glycine and serine residues. Here, we use this tabula rasa bait region to investigate several hypotheses for the triggering mechanism. When tabula rasa bait regions containing disulfide loops were elongated by reducing the disulfides, we found that A2M remained in its native c

SUBMITTER: Harwood SL

PROVIDER: S-EPMC9352918 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature

ACCESS DATA

Dataset Information

The conformational change of the protease inhibitor α₂-macroglobulin is triggered by the retraction of the cleaved bait region from a central channel.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dataset Information

The conformational change of the protease inhibitor α2-macroglobulin is triggered by the retraction of the cleaved bait region from a central channel.

OmicsDI is part of the ELIXIR infrastructure

Tweets

The conformational change of the protease inhibitor α₂-macroglobulin is triggered by the retraction of the cleaved bait region from a central channel.