1L2G

Structure of a C-terminally truncated form of glycoprotein D from HSV-1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.85 Å
  • R-Value Free: 0.297 
  • R-Value Work: 0.278 
  • R-Value Observed: 0.283 

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Ligand Structure Quality Assessment 


This is version 1.5 of the entry. See complete history


Literature

Herpes simplex virus glycoprotein D bound to the human receptor HveA.

Carfi, A.Willis, S.H.Whitbeck, J.C.Krummenacher, C.Cohen, G.H.Eisenberg, R.J.Wiley, D.C.

(2001) Mol Cell 8: 169-179

  • DOI: https://doi.org/10.1016/s1097-2765(01)00298-2
  • Primary Citation of Related Structures:  
    1JMA, 1L2G

  • PubMed Abstract: 

    Herpes simplex virus (HSV) infection requires binding of the viral envelope glycoprotein D (gD) to cell surface receptors. We report the X-ray structures of a soluble, truncated ectodomain of gD both alone and in complex with the ectodomain of its cellular receptor HveA. Two bound anions suggest possible binding sites for another gD receptor, a 3-O-sulfonated heparan sulfate. Unexpectedly, the structures reveal a V-like immunoglobulin (Ig) fold at the core of gD that is closely related to cellular adhesion molecules and flanked by large N- and C-terminal extensions. The receptor binding segment of gD, an N-terminal hairpin, appears conformationally flexible, suggesting that a conformational change accompanying binding might be part of the viral entry mechanism.


  • Organizational Affiliation

    Department of Medicine, Children's Hospital, Howard Hughes Medical Institute, 320 Longwood Avenue, Boston, MA 02115, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Glycoprotein DA,
B,
C [auth D],
D [auth C]
287Human alphaherpesvirus 1Mutation(s): 0 
UniProt
Find proteins for P57083 (Human herpesvirus 1 (strain Patton))
Explore P57083 
Go to UniProtKB:  P57083
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP57083
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.85 Å
  • R-Value Free: 0.297 
  • R-Value Work: 0.278 
  • R-Value Observed: 0.283 
  • Space Group: P 4
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 131.416α = 90
b = 131.416β = 90
c = 83.265γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
TRUNCATEdata reduction
AMoREphasing
CNSrefinement
CCP4data scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-12-16
    Type: Initial release
  • Version 1.1: 2008-04-28
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Non-polymer description, Version format compliance
  • Version 1.3: 2018-05-30
    Changes: Data collection, Derived calculations
  • Version 1.4: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Data collection, Database references, Derived calculations, Structure summary
  • Version 1.5: 2023-08-16
    Changes: Data collection, Database references, Refinement description, Structure summary