Related Experiment Video
Updated: May 10, 2026

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
Published on: November 7, 2013
Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin
Michael C Brothers1, Brett Geissler, Grant S Hisao
1Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA.
Abstract:
(1)H, (13)C, and (15)N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99% of all backbone and side-chain carbon atoms, including 99% of all backbone residues excluding proline amide nitrogens. Secondary chemical shift analysis using TALOS+ demonstrates four helices, which align with those observed within the MLD in the crystal structure of the C-terminus of PMT (PDB 2EBF) and confirm the use of the available crystal structures as templates for the isolated MLDs.
Related Concept Videos
Bacterial Toxins
Tail-anchoring of Proteins in the ER Membrane
Multi-pass Transmembrane Proteins and β-barrels
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Transducer Mechanism: Enzyme-Linked Receptors
Major types that are helpful drug targets include:
