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PDBsum entry 1h3p
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Immunoglobulin
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PDB id
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1h3p
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural and functional characterization of a monoclonal antibody specific for the pres1 region of hepatitis b virus.
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Authors
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J.C.Pizarro,
B.Vulliez-Le normand,
M.M.Riottot,
A.Budkowska,
G.A.Bentley.
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Ref.
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FEBS Lett, 2001,
509,
463-468.
[DOI no: ]
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PubMed id
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Abstract
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The monoclonal antibody 5a19, raised against the ay serotype of hepatitis B
virus, binds to the segment of the preS1 region comprising residues 37-43, which
is implicated in attachment of the virus to hepatocytes. The dissociation
constant, derived from kinetic studies using surface plasmon resonance
techniques, is in the low nanomolar range. The nucleotide sequence of the
variable domains has been determined and the corresponding germ-line genes have
been identified. The three-dimensional structure of the Fab fragment has been
determined by X-ray crystallography to 2.6 A resolution.
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Figure 1.
Fig. 1. Epitope mapping of 5a19 using the SPOTs test. The
intensity of the spot indicates the avidity of the antibody. (a)
Recognition of 6–15-mer peptides spanning the sequence 31–47
of the preS1 region (ay serotype). (b) The specificity of 5a19
was examined by substitution of each serotype-dependent residue
by the one corresponding to the ad serotype (Gly35, Ser38,
Asn39). See Section 3 for other mutations made at positions 36,
38 and 39.
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Figure 3.
Fig. 3. A stereo view of the antigen-binding site of mAb
5a19, with V[H] on the left and V[L] on the right. Upper panel:
surface representation with color coded for electrostatic
potential, with red for negative charge and blue for positive
charge. Lower panel: conformation of the antigen-binding loops,
with CDR-1 in green, CDR-2 in mauve and CDR-3 in yellow. The
figures were prepared with GRASP [21] and VMD [22], and both
rendered with Raster3D [23].
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
FEBS Lett
(2001,
509,
463-468)
copyright 2001.
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