8H0U

AQEE-30 in a DPC solution

8H0U の概要

• エントリーDOI: 10.2210/pdb8h0u/pdb
• 分子名称: AQEE-30 (1 entity in total)
• 機能のキーワード: vgf, dpc, neuropeptide
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3800.08

構造登録者

Park, O.-S.,Jeon, Y.H.,Cheong, C. (登録日: 2022-09-30, 公開日: 2022-12-14, 最終更新日: 2024-05-15)

主引用文献

Park, O.S.,Bang, J.K.,Cheong, C.,Jeon, Y.H.
Structure of AQEE-30 of VGF Neuropeptide in Membrane-Mimicking Environments.
Int J Mol Sci, 23:-, 2022

PubMed Abstract: AQEE-30 is one of the VGF peptides, which are derived from the VGF polypeptide precursor, and related to various physiological phenomena including neuroprotective effects in Huntington's disease and amyotrophic lateral sclerosis (ALS). Although various functions of AQEE-30 have been reported so far, the structure of this peptide has not been reported yet. In this study, the structure of human AQEE-30 was investigated in hexafluoroisopropanol (HFIP) and dodecyl phosphocholine (DPC) micelle solutions, using circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy. CD results showed that AQEE-30 had a partial helical structure in aqueous buffer, and the helical structure was stabilized in the HFIP and DPC micelle solutions. The 3D structures determined by NMR spectroscopy showed that AQEE-30 adopted mainly α-helical structure in both the HFIP and DPC micelle solutions. The surface of AQEE-30 showed that it was predominantly negatively charged. The residues from 601 to 611 in both the HFIP and DPC micelle solutions showed amphiphilicity with four negatively charged residues, glutamate. The C-terminal consecutive arginine residues formed a partial positively charged surface. These results suggest an α-helical active structure of AQEE-30 in the cell-membrane environment.

PubMed: 36430431
DOI: 10.3390/ijms232213953

実験手法

SOLUTION NMR