# NMR assignments of the human homodimeric mitochondrial ATP synthase inhibitor IF1

## TL;DR

This paper reports NMR assignments for human IF1, a protein that inhibits mitochondrial ATP synthase, providing insights for future drug development.

## Contribution

The study provides the first NMR assignments for the mature dimeric form of human IF1, revealing its structural characteristics.

## Key findings

- The N-terminal half of IF1 is intrinsically disordered, while the C-terminal half forms a continuous α-helix.
- NMR assignments for human IF1 will support future drug screening and structural studies.

## Abstract

ATPase inhibitory factor 1 (IF1) is the only known endogenous, proteinaceous inhibitor of mitochondrial ATP synthase in mammals. The inhibitor forms an antiparallel coiled-coil, which binds ATP synthase through an N-terminal a-helix extension that is disordered in the free protein. Because the IF1 dimer affects mitochondrial bioenergetics through its modulation of ATP synthase, it is a therapeutic target for cancer and cardiac disease. Here, we report 1H, 13C and 15N NMR assignments for the mature dimeric form of human IF1. Secondary structure analyses based on chemical shifts and short-range NOE patterns indicate the N-terminal half of the 81-residue IF1 is intrinsically disordered, while the C-terminal half adopts a continuous α-helix. The chemical shift assignments for human IF1 provide a foundation for future mechanistic structure-function studies and NMR-based drug screening.