5NWW

NMR assignment and structure of a peptide derived from the fusion peptide of HIV-1 gp41 in the presence of dodecylphosphocholine micelles

5NWW の概要

• エントリーDOI: 10.2210/pdb5nww/pdb
• NMR情報: BMRB: 34134
• 分子名称: scrFP-tag,Gp41 (1 entity in total)
• 機能のキーワード: envelope glycoprotein gp41, fusion peptide, viral protein, structure from cyana 2.1
• 由来する生物種: Human immunodeficiency virus 1; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3822.41

構造登録者

Jimenez, M.A.,Serrano, S.,Nieva, J.L.,Huarte, N. (登録日: 2017-05-08, 公開日: 2017-12-06, 最終更新日: 2024-10-16)

主引用文献

Serrano, S.,Huarte, N.,Rujas, E.,Andreu, D.,Nieva, J.L.,Jimenez, M.A.
Structure-Related Roles for the Conservation of the HIV-1 Fusion Peptide Sequence Revealed by Nuclear Magnetic Resonance.
Biochemistry, 56:5503-5511, 2017

PubMed Abstract: Despite extensive characterization of the human immunodeficiency virus type 1 (HIV-1) hydrophobic fusion peptide (FP), the structure-function relationships underlying its extraordinary degree of conservation remain poorly understood. Specifically, the fact that the tandem repeat of the FLGFLG tripeptide is absolutely conserved suggests that high hydrophobicity may not suffice to unleash FP function. Here, we have compared the nuclear magnetic resonance (NMR) structures adopted in nonpolar media by two FP surrogates, wtFP-tag and scrFP-tag, which had equal hydrophobicity but contained wild-type and scrambled core sequences LFLGFLG and FGLLGFL, respectively. In addition, these peptides were tagged at their C-termini with an epitope sequence that folded independently, thereby allowing Western blot detection without interfering with FP structure. We observed similar α-helical FP conformations for both specimens dissolved in the low-polarity medium 25% (v/v) 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP), but important differences in contact with micelles of the membrane mimetic dodecylphosphocholine (DPC). Thus, whereas wtFP-tag preserved a helix displaying a Gly-rich ridge, the scrambled sequence lost in great part the helical structure upon being solubilized in DPC. Western blot analyses further revealed the capacity of wtFP-tag to assemble trimers in membranes, whereas membrane oligomers were not observed in the case of the scrFP-tag sequence. We conclude that, beyond hydrophobicity, preserving sequence order is an important feature for defining the secondary structures and oligomeric states adopted by the HIV FP in membranes.

PubMed: 28930470
DOI: 10.1021/acs.biochem.7b00745

実験手法

SOLUTION NMR