PMID- 19217393
OWN - NLM
STAT- MEDLINE
DCOM- 20090427
LR  - 20211020
IS  - 0969-2126 (Print)
IS  - 1878-4186 (Electronic)
IS  - 0969-2126 (Linking)
VI  - 17
IP  - 2
DP  - 2009 Feb 13
TI  - Structure of Epstein-Barr virus glycoprotein 42 suggests a mechanism for 
      triggering receptor-activated virus entry.
PG  - 223-33
LID - 10.1016/j.str.2008.12.010 [doi]
AB  - Epstein-Barr virus requires glycoproteins gH/gL, gB, and gp42 to fuse its lipid 
      envelope with B cells. Gp42 is a type II membrane protein consisting of a 
      flexible N-terminal region, which binds gH/gL, and a C-terminal lectin-like 
      domain that binds to the B-cell entry receptor human leukocyte antigen (HLA) 
      class II. Gp42 triggers membrane fusion after HLA binding, a process that 
      requires simultaneous binding to gH/gL and a functional hydrophobic pocket in the 
      lectin domain adjacent to the HLA binding site. Here we present the structure of 
      gp42 in its unbound form. Comparisons to the previously determined structure of a 
      gp42:HLA complex reveals additional N-terminal residues forming part of the gH/gL 
      binding site and structural changes in the receptor binding domain. Although the 
      core of the lectin domain remains similar, significant shifts in two loops and an 
      alpha helix bordering the essential hydrophobic pocket suggest a structural 
      mechanism for triggering fusion.
FAU - Kirschner, Austin N
AU  - Kirschner AN
AD  - Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern 
      University, Evanston, IL 60208, USA.
FAU - Sorem, Jessica
AU  - Sorem J
FAU - Longnecker, Richard
AU  - Longnecker R
FAU - Jardetzky, Theodore S
AU  - Jardetzky TS
LA  - eng
GR  - R01 CA117794/CA/NCI NIH HHS/United States
GR  - T32 AI060523/AI/NIAID NIH HHS/United States
GR  - R01 CA117794-02/CA/NCI NIH HHS/United States
GR  - R01 CA093444/CA/NCI NIH HHS/United States
GR  - R01 AI076183-06A2/AI/NIAID NIH HHS/United States
GR  - CA117794/CA/NCI NIH HHS/United States
GR  - R01 CA117794-01A1/CA/NCI NIH HHS/United States
GR  - 5 T32 GM008152/GM/NIGMS NIH HHS/United States
GR  - R01 CA117794-05/CA/NCI NIH HHS/United States
GR  - R01 CA117794-03/CA/NCI NIH HHS/United States
GR  - T32 GM008152/GM/NIGMS NIH HHS/United States
GR  - R01 AI076183-07/AI/NIAID NIH HHS/United States
GR  - R01 CA117794-04/CA/NCI NIH HHS/United States
GR  - R01 AI076183-09/AI/NIAID NIH HHS/United States
GR  - CA93444/CA/NCI NIH HHS/United States
GR  - R01 AI076183-08/AI/NIAID NIH HHS/United States
GR  - R01 AI076183/AI/NIAID NIH HHS/United States
GR  - R01 CA117794-06/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PL  - United States
TA  - Structure
JT  - Structure (London, England : 1993)
JID - 101087697
RN  - 0 (HLA Antigens)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Viral Proteins)
SB  - IM
CIN - Structure. 2009 Feb 13;17(2):147-9. PMID: 19217384
MH  - Animals
MH  - B-Lymphocytes/metabolism/virology
MH  - Binding Sites
MH  - CHO Cells
MH  - Cells, Cultured
MH  - Cricetinae
MH  - Cricetulus
MH  - HLA Antigens/*metabolism
MH  - Herpesvirus 4, Human/*chemistry/*physiology
MH  - Membrane Glycoproteins/chemistry/metabolism/physiology
MH  - Models, Biological
MH  - Models, Molecular
MH  - Protein Binding
MH  - Protein Conformation
MH  - Protein Interaction Domains and Motifs
MH  - Spodoptera
MH  - Viral Proteins/*chemistry/metabolism/physiology
MH  - *Virus Internalization
PMC - PMC3085316
MID - NIHMS96458
EDAT- 2009/02/17 09:00
MHDA- 2009/04/28 09:00
PMCR- 2011/05/02
CRDT- 2009/02/17 09:00
PHST- 2008/09/15 00:00 [received]
PHST- 2008/11/24 00:00 [revised]
PHST- 2008/12/10 00:00 [accepted]
PHST- 2009/02/17 09:00 [entrez]
PHST- 2009/02/17 09:00 [pubmed]
PHST- 2009/04/28 09:00 [medline]
PHST- 2011/05/02 00:00 [pmc-release]
AID - S0969-2126(09)00025-2 [pii]
AID - 10.1016/j.str.2008.12.010 [doi]
PST - ppublish
SO  - Structure. 2009 Feb 13;17(2):223-33. doi: 10.1016/j.str.2008.12.010.