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Updated: Feb 19, 2026

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
Published on: March 5, 2017
Kinetoplastid membrane protein-11 adopts a four-helix bundle fold in DPC micelle
Liang Zhong Lim1, Shermaine Ee1, Jing Fu1
1Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore.
Abstract:
Kinetoplastid membrane protein-11 (KMP11) is a membrane-associated surface protein of kinetoplastids, which has a strong antigenicity but no mammalian homolog, thus representing a promising vaccine candidate. Here, by CD and NMR, we revealed that in buffer, KMP11 assumes a highly helical conformation without stable tertiary packing. Remarkably, upon interacting with dodecylphosphocholine (DPC) micelle, despite minor changes in secondary structures, KMP11 undergoes rearrangements to form a defined structure. We found that its three-dimensional structure unexpectedly adopts the classic four-helix bundle fold. The surface constituted by the N-/C-termini and conserved loop was characterized to dynamically interact with the polar phase of DPC micelle. Our results provide a structural basis for understanding KMP11 functions and further offer a promising avenue for engineering better vaccines.
Database:
The structure coordinate of KMP11 in DPC micelle has been deposited in PDB with ID of 5Y70 and the associated NMR data were deposited in BMRB with ID of 36112.
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