Title
Kinetoplastid membrane protein‐11 adopts a four‐helix bundle fold in DPC micelle
Author
Liang Zhong Lim, Shermaine Ee, Jing Fu, Yanming Tan, Cynthia Y. He, Jianxing Song
Year
2017
Journal
FEBS Letters
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.
Instrument
J-1500
Keywords
Circular dichroism, Secondary structure, Tertiary structure, Membrane interactions, Biochemistry