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PDBsum entry 1ggc
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Immunoglobulin
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PDB id
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1ggc
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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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Major antigen-Induced domain rearrangements in an antibody.
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Authors
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R.L.Stanfield,
M.Takimoto-Kamimura,
J.M.Rini,
A.T.Profy,
I.A.Wilson.
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Ref.
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Structure, 1993,
1,
83-93.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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BACKGROUND: Recent structural results have shown that antibodies use an induced
fit mechanism to recognize and bind their antigens. Here we present the
crystallographically determined structure of an Fab directed against an HIV-1
peptide (Fab 50.1) in the unliganded state and compare it with the peptide-bound
structure. We perform a detailed analysis of the components that contribute to
enhanced antigen binding and recognition. RESULTS: Induced fit of Fab 50.1 to
its peptide antigen involves a substantial rearrangement of the third
complementarity determining region loop of the heavy chain (H3), as well as a
large rotation of the variable heavy (VH) chain relative to the variable light
(VL) chain. Analysis of other Fab structures suggests that the extent of the
surface area buried at the VL-VH interface correlates with the ability to alter
antibody quaternary structure by reorientation of the VL-VH domains. CONCLUSION:
Fab 50.1 exhibits the largest conformational changes yet observed in a single
antibody. These can be attributed to the flexibility of the variable region.
Comparisons of new data with previous examples lend to the general conclusion
that a small VL-VH interface, due in part to a short H3 loop, permits
substantial alterations to the antigen-binding pocket. This has major
implications for the prediction, engineering and design of antibody-combining
sites.
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Secondary reference #1
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Title
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Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, In complex with its v3 loop peptide antigen.
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Authors
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J.M.Rini,
R.L.Stanfield,
E.A.Stura,
P.A.Salinas,
A.T.Profy,
I.A.Wilson.
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Ref.
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Proc Natl Acad Sci U S A, 1993,
90,
6325-6329.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Crystallization, Sequence, And preliminary crystallographic data for an antipeptide FAB 50.1 and peptide complexes with the principal neutralizing determinant of HIV-1 gp120.
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Authors
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E.A.Stura,
R.L.Stanfield,
G.G.Fieser,
S.Silver,
M.Roguska,
L.M.Hincapie,
H.K.Simmerman,
A.T.Profy,
I.A.Wilson.
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Ref.
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Proteins, 1992,
14,
499-508.
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PubMed id
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