Crystal structure of adenovirus E3-19K bound to HLA-A2 reveals mechanism for immunomodulation.
Crystal structure of adenovirus E3-19K bound to HLA-A2 reveals mechanism for immunomodulation.
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DOI:
10.1038/nsmb.2396
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发表时间:
2012-11
影响因子:
16.8
通讯作者:
Bouvier, Marlene
中科院分区:
文献类型:
--
作者:
Li, Lenong;Muzahim, Yasameen;Bouvier, Marlene
E3-19K binds to and retains MHC class I molecules in the endoplasmic reticulum, suppressing anti-Adenovirus (Ad) activities of T-cells. We determined the structure of the Ad serotype 2 (Ad2, species C) E3-19K–HLA-A2 complex to 1.95 Å resolution. Ad2 E3-19K binds to the N-terminus of the HLA-A2 groove, contacting the α1-, α2-, and α3-domains and β2m. Ad2 E3-19K has a unique structure comprised of a large N-terminal domain, formed by two partially overlapping β-sheets arranged in a V-shape, a C-terminal α-helix and tail. The structure reveals determinants in E3-19K and HLA-A2 that are important for complex formation; conservation of some of these determinants in E3-19K proteins of different species and MHC I of different loci suggests a universal binding mode for all E3-19K proteins. Our structure is important for understanding the immunomodulatory function of E3-19K.
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DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
影响因子:
14.9
作者:
Holm, L;Sander, C
通讯作者:
Sander, C
DOI:
10.1107/s0907444992007698
发表时间:
1993-01-01
期刊:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子:
--
作者:
COWTAN, KD;MAIN, P
通讯作者:
MAIN, P
影响因子:
5.4
作者:
FLOMENBERG, P;SZMULEWICZ, J;LUPATKIN, H
通讯作者:
LUPATKIN, H
DOI:
10.1107/s0907444998003254
发表时间:
1998-09-01
期刊:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子:
--
作者:
Brunger, AT;Adams, PD;Warren, GL
通讯作者:
Warren, GL