Polarized benzene rings can promote the interaction between CaM and the CaMBD region of nNOS.

ABSTRACT:

Introduction

The neuronal nitric oxide synthase (nNOS) subtype of nitric oxide synthase (NOS) is an enzyme required for learning and memory. Overactivation of nNOS can lead to oxidative/nitrite stress, which is complicit in the pathophysiology of various neurological and psychiatric disorders. Previous studies have shown that calmodulin (CaM) forms complexes with Ca²⁺ and binds to the calmodulin-binding domain (CaMBD) of nNOS, thereby upregulating its catalytic activity in hippocampal neurons. To date, there has been no explanation for the non-covalent interactions in the CaMBD-CaM binding structure model of nNOS.

Methods

In this study, we aimed to investigate the intrinsic factors involved in the binding of CaM to NOS-CaMBD and designed interfering peptides based

SUBMITTER: Wan W 

PROVIDER: S-EPMC11405375 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature