2DCI

NMR structure of influenza HA fusion peptide mutant W14A in DPC in pH5

2DCI の概要

• エントリーDOI: 10.2210/pdb2dci/pdb
• 関連するPDBエントリー: 1IBN 1IBO 1XOO 1XOP
• NMR情報: BMRB: 6954
• 分子名称: Hemagglutinin (1 entity in total)
• 機能のキーワード: ha, fusion peptide, viral protein
• 細胞内の位置: Virion membrane; Single-pass type I membrane protein (Potential): P11134
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1939.15

構造登録者

Tamm, L.K.,Lai, A.L. (登録日: 2006-01-07, 公開日: 2006-01-24, 最終更新日: 2024-05-29)

主引用文献

Lai, A.L.,Park, H.,White, J.M.,Tamm, L.K.
Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity
J.Biol.Chem., 281:5760-5770, 2006

PubMed Abstract: The fusion peptide of influenza hemagglutinin is crucial for cell entry of this virus. Previous studies showed that this peptide adopts a boomerang-shaped structure in lipid model membranes at the pH of membrane fusion. To examine the role of the boomerang in fusion, we changed several residues proposed to stabilize the kink in this structure and measured fusion. Among these, mutants E11A and W14A expressed hemagglutinins with hemifusion and no fusion activities, and F9A and N12A had no effect on fusion, respectively. Binding enthalpies and free energies of mutant peptides to model membranes and their ability to perturb lipid bilayer structures correlated well with the fusion activities of the parent full-length molecules. The structure of W14A determined by NMR and site-directed spin labeling features a flexible kink that points out of the membrane, in sharp contrast to the more ordered boomerang of the wild-type, which points into the membrane. A specific fixed angle boomerang structure is thus required to support membrane fusion.

PubMed: 16407195
DOI: 10.1074/jbc.M512280200

実験手法

SOLUTION NMR