The Model Structures of the Complement Component 5a Receptor (C5aR) Bound to the Native and Engineered ^hC5a.

ABSTRACT: The interaction of ^hC5a with C5aR, previously hypothesized to involve a "two-site" binding, (i) recognition of the bulk of ^hC5a by the N-terminus (NT) of C5aR ("site1"), and (ii) recognition of C-terminus (CT) of ^hC5a by the extra cellular surface (ECS) of the C5aR ("site2"). However, the pharmacological landscapes of such recognition sites are yet to be illuminated at atomistic resolution. In the context, unique model complexes of C5aR, harboring pharmacophores of diverse functionality at the "site2" has recently been described. The current study provides a rational illustration of the "two-site" binding paradigm in C5aR, by recruiting the native agonist ^hC5a and engineered antagonist ^hC5a(A8). The ^hC5a-C5aR and ^h

SUBMITTER: Sahoo AR 

PROVIDER: S-EPMC5811428 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature