Designed leucine-rich repeat proteins bind two muramyl dipeptide ligands.

ABSTRACT: Designed protein receptors hold diagnostic and therapeutic promise. We now report the design of five consensus leucine-rich repeat proteins (CLRR4-8) based on the LRR domain of nucleotide-binding oligomerization domain (NOD)-like receptors involved in the innate immune system. The CLRRs bind muramyl dipeptide (MDP), a bacterial cell wall component, with micromolar affinity. The overall K_{d app} values ranged from 1.0 to 57 μM as measured by fluorescence quenching experiments. Biphasic fluorescence quenching curves were observed in all CLRRs, with higher affinity K_d1 values ranging from 0.04 to 4.5 μM, and lower affinity K_d2 values ranging from 3.1 to 227 μM. These biphasic binding curves, along with the docking studies of MDP binding to CLRR4, suggest that at

SUBMITTER: Kim CS 

PROVIDER: S-EPMC7980508 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature