Download MendeleyKinetoplastid membrane protein-11 adopts a four-helix bundle fold in DPC micelle.
Lim, L.Z., Ee, S., Fu, J., Tan, Y., He, C.Y., Song, J.(2017) FEBS Lett 591: 3793-3804
- PubMed: 29082514
- DOI: https://doi.org/10.1002/1873-3468.12891
- Primary Citation of Related Structures:
5Y70 - PubMed 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.
Organizational Affiliation:
Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore.
