Hydrophobic ligands influence the structure, stability, and processing of the major cockroach allergen Bla g 1.

ABSTRACT: The cockroach allergen Bla g 1 forms a novel fold consisting of 12 amphipathic alpha-helices enclosing an exceptionally large hydrophobic cavity which was previously demonstrated to bind a variety of lipids. Since lipid-dependent immunoactivity is observed in numerous allergens, understanding the structural basis of this interaction could yield insights into the molecular determinants of allergenicity. Here, we report atomic modelling of Bla g 1 bound to both fatty-acid and phospholipids ligands, with 8 acyl chains suggested to represent full stoichiometric binding. This unusually high occupancy was verified experimentally, though both modelling and circular dichroism indicate that the general alpha-helical structure is maintained regardless of cargo loading. Fatty-acid cargoes significant

SUBMITTER: Foo ACY 

PROVIDER: S-EPMC6893020 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature