1A7L

DOMINANT B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS IN THE FORM OF AN INSERTED PEPTIDE SEGMENT IN MALTODEXTRIN-BINDING PROTEIN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.286 
  • R-Value Work: 0.192 
  • R-Value Observed: 0.192 

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This is version 2.1 of the entry. See complete history


Literature

Crystal structure of a dominant B-cell epitope from the preS2 region of hepatitis B virus in the form of an inserted peptide segment in maltodextrin-binding protein.

Saul, F.A.Vulliez-le Normand, B.Lema, F.Bentley, G.A.

(1998) J Mol Biol 280: 185-192

  • DOI: https://doi.org/10.1006/jmbi.1998.1866
  • Primary Citation of Related Structures:  
    1A7L

  • PubMed Abstract: 

    We report here the crystal structure of MalE-B363, a recombinant construction of maltodextrin-binding protein bearing a dominant B-cell epitope sequence from the preS2 region of the hepatitis B surface antigen. The inserted peptide sequence, which replaces the seven carboxy-terminal residues of maltodextrin-binding protein, carries the 14 amino acid residue epitope contained between residues 132 and 145 from the preS2 region. The epitope sequence is flanked on either side by additional residues that result from the genetically engineered insertion, bringing the total length of the foreign peptide to 26 amino acid residues. The hybrid protein has been previously shown to be recognised by monoclonal antibodies elicited by the native viral antigen. Three independent molecules of MalE-B363 are present in the asymmetric unit of the crystal. All 14 epitope residues could be traced for one molecule, ten epitope residues had significant electron density for the second, but no density was visible for the epitope of the third. The conformation of the amino-terminal segment of the epitope from Gln132(e) to Gly138(e) is similar in the two molecules of MalE-B363 for which the foreign peptide could be traced. Moreover, the conformation of a smaller segment, comprising residues Asp133(e) to Arg137(e), is similar to that present in the previously determined crystal structure of MalE-B133, another insertion/deletion mutant of maltodextrin-binding protein bearing the preS2 epitope. The presence of a common structural motif for the same sequence in disparate molecular environments suggests that this conformation might be present also in the native viral antigen. This could provide a structural basis to explain the cross-reactivity of anti-preS2 monoclonal antibodies with these hybrid proteins.


  • Organizational Affiliation

    C.N.R.S. U.R.A. 1961, Institut Pasteur, 25 rue du Dr. Roux, Paris cedex 15, 75724, France.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MALE-B363
A, B, C
389synthetic constructMutation(s): 0 
Gene Names: MBP MUTANT
UniProt
Find proteins for P0AEX9 (Escherichia coli (strain K12))
Explore P0AEX9 
Go to UniProtKB:  P0AEX9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0AEX9
Sequence Annotations
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  • Reference Sequence
Oligosaccharides

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Entity ID: 2
MoleculeChains Length2D Diagram Glycosylation3D Interactions
alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
D, E, F
2N/A
Glycosylation Resources
GlyTouCan:  G07411ON
GlyCosmos:  G07411ON
Biologically Interesting Molecules (External Reference) 1 Unique
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.286 
  • R-Value Work: 0.192 
  • R-Value Observed: 0.192 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 64.6α = 90
b = 71.3β = 94.9
c = 123.2γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
XDSdata reduction
MARSCALEdata scaling
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-06-17
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Advisory, Atomic model, Data collection, Derived calculations, Non-polymer description, Other, Structure summary
  • Version 2.1: 2023-08-02
    Changes: Database references, Refinement description, Structure summary