5Y70

NMR structure of KMP11 in DPC micelle

5Y70 の概要

• エントリーDOI: 10.2210/pdb5y70/pdb
• NMR情報: BMRB: 36112
• 分子名称: Kinetoplastid membrane protein 11 (1 entity in total)
• 機能のキーワード: dpc micelle, kinetoplastid membrane protein-11, trypanosomes, membrane protein
• 由来する生物種: Trypanosoma brucei brucei
• 細胞内の位置: Cytoplasm, cytoskeleton : P69300
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12071.57

構造登録者

Lu, Y.,Lim, L.Z.,Song, J. (登録日: 2017-08-16, 公開日: 2018-02-07, 最終更新日: 2024-05-15)

主引用文献

Lim, L.Z.,Ee, S.,Fu, J.,Tan, Y.,He, C.Y.,Song, J.
Kinetoplastid membrane protein-11 adopts a four-helix bundle fold in DPC micelle.
FEBS Lett., 591:3793-3804, 2017

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.

PubMed: 29082514
DOI: 10.1002/1873-3468.12891

実験手法

SOLUTION NMR