Altered backbone and side-chain interactions result in route heterogeneity during the folding of interleukin-1β (IL-1β).

ABSTRACT: Deletion of the β-bulge trigger-loop results in both a switch in the preferred folding route, from the functional loop packing folding route to barrel closure, as well as conversion of the agonist activity of IL-1β into antagonist activity. Conversely, circular permutations of IL-1β conserve the functional folding route as well as the agonist activity. These two extremes in the folding-functional interplay beg the question of whether mutations in IL-1β would result in changes in the populations of heterogeneous folding routes and the signaling activity. A series of topologically equivalent water-mediated β-strand bridging interactions within the pseudosymmetric β-trefoil fold of IL-1β highlight the backbone water interactions that stabilize the secondary and tertiary structure of the prote

SUBMITTER: Capraro DT 

PROVIDER: S-EPMC3752112 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature