3 years ago

Kinetoplastid membrane protein-11 adopts a four-helix bundle fold in DPC micelle

Jianxing Song, Yanming Tan, Shermaine Ee, Yingxin He, Jing Fu, Liang Zhong Lim
KMP11 is a membrane-associated surface protein of kinetoplastids, which has a strong antigenicity but no mammalian homologue, 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 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. This article is protected by copyright. All rights reserved.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/1873-3468.12891

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