Resonance assignments of the human receptor interacting protein kinase 1 (RIPK1) in its fibrillar conformation.

Abstract

Receptor-interacting protein kinase 1 (RIPK1) is a key regulator of necroptotic signalling that forms functional amyloid fibrils through its RIP Homotypic Interaction Motif (RHIM). Here, we report the solid-state NMR chemical shift assignments for the rigid amyloid core of human RIPK1 fibrils, encompassing residues 529-552 within the RHIM. Assignments were obtained from uniformly ¹³C,¹⁵N-labeled protein diluted with unlabeled protein and measured using cross-polarization magic angle spinning (CPMAS) experiments on a cryogenic probe. The dataset includes backbone and side-chain resonances for the ordered region and provides a basis for high-resolution structural and dynamics studies of RIPK1 and related RHIM-containing assemblies.