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Kinetoplastid membrane protein‐11 adopts a four‐helix bundle fold in DPC micelle
Author(s) -
Lim Liang Zhong,
Ee Shermaine,
Fu Jing,
Tan Yanming,
He Cynthia Y.,
Song Jianxing
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12891
Subject(s) - helix bundle , fold (higher order function) , chemistry , micelle , bundle , helix (gastropod) , biophysics , biochemistry , protein structure , biology , materials science , computer science , aqueous solution , snail , composite material , programming language , ecology
Kinetoplastid membrane protein‐11 ( KMP 11) 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, KMP 11 assumes a highly helical conformation without stable tertiary packing. Remarkably, upon interacting with dodecylphosphocholine ( DPC ) micelle, despite minor changes in secondary structures, KMP 11 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 KMP 11 functions and further offer a promising avenue for engineering better vaccines. Database The structure coordinate of KMP 11 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