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PDBsum entry 1f90
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Immune system
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PDB id
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1f90
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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 an anti-Interleukin-2 monoclonal antibody FAB complexed with an antigenic nonapeptide.
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Authors
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P.V.Afonin,
A.V.Fokin,
I.N.Tsygannik,
I.Y.Mikhailova,
L.V.Onoprienko,
I.I.Mikhaleva,
V.T.Ivanov,
T.Y.Mareeva,
V.A.Nesmeyanov,
N.Li,
W.A.Pangborn,
W.L.Duax,
V.Z.Pletnev.
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Ref.
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Protein Sci, 2001,
10,
1514-1521.
[DOI no: ]
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PubMed id
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Abstract
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The three-dimensional structure of the Fab fragment of a monoclonal antibody
(LNKB-2) to human interleukin-2 (IL-2) complexed with a synthetic antigenic
nonapeptide, Ac-Lys-Pro-Leu-Glu-Glu-Val-Leu-Asn-Leu-OMe, has been determined at
3.0 A resolution. In the structure, four out of the six hypervariable loops of
the Fab (complementarity determining regions [CDRs] L1, H1, H2, and H3) are
involved in peptide association through hydrogen bonding, salt bridge formation,
and hydrophobic interactions. The Tyr residues in the Fab antigen binding site
play a major role in antigen-antibody recognition. The structures of the
complexed and uncomplexed Fab were compared. In the antigen binding site the
CDR-L1 loop of the antibody shows the largest structural changes upon peptide
binding. The peptide adopts a mostly alpha-helical conformation similar to that
in the epitope fragment 64-72 of the IL-2 antigen. The side chains of residues
Leu 66, Val 69, and Leu 70, which are shielded internally in the IL-2 structure,
are involved in interactions with the Fab in the complex studied. This indicates
that antibody-antigen complexation involves a significant rearrangement of the
epitope-containing region of the IL-2 with retention of the alpha-helical
character of the epitope fragment.
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Secondary reference #1
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Title
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[Spatial structure of a FAB-Fragment of a monoclonal antibody to human interleukin-2 in two crystalline forms at a resolution of 2.2 and 2.9 angstroms].
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Authors
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A.V.Fokin,
P.V.Afonin,
I.I.U.Mikhaĭlova,
I.N.Tsygannik,
T.I.U.Mareeva,
V.A.Nesmeianov,
W.Pangborn,
N.Lee,
W.Duax,
E.Siszak,
V.Z.Pletnev.
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Ref.
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Bioorg Khim, 2000,
26,
571-578.
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PubMed id
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