6SP2

CryoEM structure of SERINC from Drosophila melanogaster

6SP2 の概要

• エントリーDOI: 10.2210/pdb6sp2/pdb
• EMDBエントリー: 10277 10279
• 分子名称: Membrane protein TMS1d, Lauryl Maltose Neopentyl Glycol, O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine, ... (4 entities in total)
• 機能のキーワード: anti-retroviral, tm10, serinc fold, novel fold, membrane protein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 353929.39

構造登録者

Pye, V.E.,Nans, A.,Cherepanov, P. (登録日: 2019-08-30, 公開日: 2020-01-01, 最終更新日: 2024-11-06)

主引用文献

Pye, V.E.,Rosa, A.,Bertelli, C.,Struwe, W.B.,Maslen, S.L.,Corey, R.,Liko, I.,Hassall, M.,Mattiuzzo, G.,Ballandras-Colas, A.,Nans, A.,Takeuchi, Y.,Stansfeld, P.J.,Skehel, J.M.,Robinson, C.V.,Pizzato, M.,Cherepanov, P.
A bipartite structural organization defines the SERINC family of HIV-1 restriction factors.
Nat.Struct.Mol.Biol., 27:78-83, 2020

PubMed Abstract: The human integral membrane protein SERINC5 potently restricts HIV-1 infectivity and sensitizes the virus to antibody-mediated neutralization. Here, using cryo-EM, we determine the structures of human SERINC5 and its orthologue from Drosophila melanogaster at subnanometer and near-atomic resolution, respectively. The structures reveal a novel fold comprised of ten transmembrane helices organized into two subdomains and bisected by a long diagonal helix. A lipid binding groove and clusters of conserved residues highlight potential functional sites. A structure-based mutagenesis scan identified surface-exposed regions and the interface between the subdomains of SERINC5 as critical for HIV-1-restriction activity. The same regions are also important for viral sensitization to neutralizing antibodies, directly linking the antiviral activity of SERINC5 with remodeling of the HIV-1 envelope glycoprotein.

PubMed: 31907454
DOI: 10.1038/s41594-019-0357-0

実験手法

ELECTRON MICROSCOPY (3.33 Å)