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PDBsum entry 1frg
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Viral protein/immune system
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PDB id
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1frg
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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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Crystal structure of a peptide complex of anti-Influenza peptide antibody FAB 26/9. Comparison of two different antibodies bound to the same peptide antigen.
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Authors
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M.E.Churchill,
E.A.Stura,
C.Pinilla,
J.R.Appel,
R.A.Houghten,
D.H.Kono,
R.S.Balderas,
G.G.Fieser,
U.Schulze-Gahmen,
I.A.Wilson.
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Ref.
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J Mol Biol, 1994,
241,
534-556.
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PubMed id
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Abstract
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The three-dimensional structure of the complex of a second anti-peptide antibody
(Fab 26/9) that recognizes the same six-residue epitope of an immunogenic
peptide from influenza virus hemagglutinin (HA1; 75-110) as Fab 17/9 with the
peptide has been determined at 2.8 A resolution. The amino acid sequence of the
variable region of the 26/9 antibody differs in 24 positions from that of 17/9,
the first antibody in this series for which several ligand-bound and free
structures have been determined and refined. Comparison of the 26/9-peptide with
the 17/9-peptide complex structures shows that the two Fabs are very similar
(r.m.s.d. 0.5 to 0.8 A) and that the peptide antigen (101-107) has virtually the
same conformation (r.m.s.d. 0.3 to 0.8 A) when bound to both antibodies. A
sequence difference in the 26/9 binding pocket (L94; His in 26/9, Asn in 17/9)
results in an interaction with a bound water molecule that is not seen in the
17/9 structures. Epitope mapping shows that the relative specificity of 26/9 and
17/9 antibodies for individual positions of the peptide antigen are slightly
different. Amino acid substitutions in the peptide, particularly at position
SerP107, are tolerated to different extents by 17/9 and 26/9. Structural and
sequence analysis suggests that amino acid differences near the peptide-binding
site are responsible for altering slightly the specificity of 26/9 for three
peptide residues and illustrates how amino acid substitutions can modify
antibody-antigen interactions and thereby modulate antibody specificity.
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Secondary reference #1
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Title
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Detailed analysis of the free and bound conformations of an antibody. X-Ray structures of FAB 17/9 and three different FAB-Peptide complexes.
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Authors
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U.Schulze-Gahmen,
J.M.Rini,
I.A.Wilson.
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Ref.
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J Mol Biol, 1993,
234,
1098-1118.
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PubMed id
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Secondary reference #2
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Title
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Structural evidence for induced fit as a mechanism for antibody-Antigen recognition.
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Authors
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J.M.Rini,
U.Schulze-Gahmen,
I.A.Wilson.
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Ref.
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Science, 1992,
255,
959-965.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Preliminary crystallographic data, Primary sequence, And binding data for an anti-Peptide FAB and its complex with a synthetic peptide from influenza virus hemagglutinin.
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Authors
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U.Schulze-Gahmen,
J.M.Rini,
J.Arevalo,
E.A.Stura,
J.H.Kenten,
I.A.Wilson.
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Ref.
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J Biol Chem, 1988,
263,
17100-17105.
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PubMed id
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