期刊
VIROLOGY
卷 454, 期 -, 页码 93-101出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2014.02.015
关键词
Membrane anchor; Transmembrane helix; Amphipathic helix; Arginine snorkel; Histidine pH sensor; Type I membrane protein; Membrane fusion protein; Secondary structure prediction
类别
资金
- National Institutes of Health [P01 GM022778, R01 GM102869]
- Steitz Center for Structural Biology, Gwangju Institute of Science and Technology, Republic of Korea
- Burroughs Welcome Investigator in the Pathogenesis of Infectious Disease Award
The membrane anchors of viral envelope proteins play essential roles in cell entry. Recent crystal structures of the ectodomain of envelope protein E2 from a pestivirus suggest that E2 belongs to a novel structural class of membrane fusion machinery. Based on geometric constraints from the E2 structures, we generated atomic models of the El and E2 membrane anchors using computational approaches. The El anchor contains two amphipathic perimembrane helices and one transmembrane helix; the E2 anchor contains a short helical hairpin stabilized in the membrane by an arginine residue, similar to flaviviruses. A pair of histidine residues in the E2 ectodomain may participate in pH sensing. The proposed atomic models point to Cys987 in E2 as the site of disulfide bond linkage with El to form El E2 heterodimers. The membrane anchor models provide structural constraints for the disulfide bonding pattern and overall backbone conformation of the El ectodomain. (c) 2014 Elsevier Inc. All rights reserved.
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