Ontology highlight
ABSTRACT:
SUBMITTER: Wang B
PROVIDER: S-EPMC4859480 | biostudies-literature | 2016 May
REPOSITORIES: biostudies-literature
Wang Bochao B Nishimura Mitsuhiro M Tang Huamin H Kawabata Akiko A Mahmoud Nora F NF Khanlari Zahra Z Hamada Daizo D Tsuruta Hiroki H Mori Yasuko Y
PLoS pathogens 20160506 5
The tegument protein U14 of human herpesvirus 6B (HHV-6B) constitutes the viral virion structure and is essential for viral growth. To define the characteristics and functions of U14, we determined the crystal structure of the N-terminal domain of HHV-6B U14 (U14-NTD) at 1.85 Å resolution. U14-NTD forms an elongated helix-rich fold with a protruding β hairpin. U14-NTD exists as a dimer exhibiting broad electrostatic interactions and a network of hydrogen bonds. This is first report of the crysta ...[more]