4FHQ

Crystal Structure of HVEM


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.25 Å
  • R-Value Free: 0.292 
  • R-Value Work: 0.279 
  • R-Value Observed: 0.280 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Increased Heterologous Protein Expression in Drosophila S2 Cells for Massive Production of Immune Ligands/Receptors and Structural Analysis of Human HVEM.

Liu, W.Vigdorovich, V.Zhan, C.Patskovsky, Y.Bonanno, J.B.Nathenson, S.G.Almo, S.C.

(2015) Mol Biotechnol 57: 914-922

  • DOI: https://doi.org/10.1007/s12033-015-9881-2
  • Primary Citation of Related Structures:  
    4FHQ

  • PubMed Abstract: 

    Many immune ligands and receptors are potential drug targets, which delicately manipulate a wide range of immune responses. We describe here the successful application of an efficient method to dramatically improve the heterologous expression levels in Drosophila Schneider 2 cells, which enables the high-throughput production of several important immune ligands/receptors for raising antibodies, and for the structural and functional analyses. As an example, we purified the protein and characterized the structure of the immune receptor herpesvirus entry mediator (HVEM, TNFRSF14). HVEM is a member of tumor necrosis factor receptor superfamily, which is recognized by herpes simplex virus glycoprotein D (gD) and facilitates viral entry. HVEM participates in a range of interactions with other cell surface molecules, including LIGHT, BTLA, and CD160 to modulate a wide range of immune processes in CD4(+) and CD8(+) T cells, as well as NK cells. Due to the involvement of HVEM in these diverse signaling interactions, crystal structures of HVEM in complex with gD or BTLA have been previously reported. Here, we report the structure of HVEM in the absence of any ligands.


  • Organizational Affiliation

    Department of Cell Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY, 10461, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Tumor necrosis factor receptor superfamily member 14134Homo sapiensMutation(s): 0 
Gene Names: HVEAHVEMTNFRSF14UNQ329/PRO509
UniProt & NIH Common Fund Data Resources
Find proteins for Q92956 (Homo sapiens)
Explore Q92956 
Go to UniProtKB:  Q92956
PHAROS:  Q92956
GTEx:  ENSG00000157873 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ92956
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.25 Å
  • R-Value Free: 0.292 
  • R-Value Work: 0.279 
  • R-Value Observed: 0.280 
  • Space Group: I 4 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 94.736α = 90
b = 94.736β = 90
c = 77.159γ = 90
Software Package:
Software NamePurpose
CBASSdata collection
PHASERphasing
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2012-07-18
    Type: Initial release
  • Version 1.1: 2012-07-25
    Changes: Structure summary
  • Version 1.2: 2015-09-02
    Changes: Database references
  • Version 1.3: 2015-09-16
    Changes: Database references
  • Version 1.4: 2023-09-13
    Changes: Data collection, Database references, Refinement description