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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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PDB id:
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Immune system
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Title:
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Fab fragment of monoclonal antibody (lnkb-2) against human interleukin-2 in complex with antigenic peptide
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Structure:
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Fab fragment of monoclonal antibody. Chain: l. Fab fragment of monoclonal antibody. Chain: h. Antigenic nonapeptide. Chain: e. Engineered: yes
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Cell_line: hybridoma. Synthetic: yes. Other_details: the peptide was chemically synthetized in solution
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Biol. unit:
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Trimer (from
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Resolution:
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2.60Å
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R-factor:
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0.165
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R-free:
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0.245
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Authors:
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P.V.Afonin,A.V.Fokin,I.N.Tsigannik,I.Y.Mikhailova,L.V.Onoprienko, I.I.Mikhaleva,V.T.Ivanov,T.Y.Mareeva,V.A.Nesmeyanov,N.Li,W.L.Duax, V.Z.Pletnev
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Key ref:
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P.V.Afonin
et al.
(2001).
Crystal structure of an anti-interleukin-2 monoclonal antibody Fab complexed with an antigenic nonapeptide.
Protein Sci,
10,
1514-1521.
PubMed id:
DOI:
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Date:
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06-Jul-00
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Release date:
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11-Jul-01
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PROCHECK
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Headers
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References
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DOI no:
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Protein Sci
10:1514-1521
(2001)
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PubMed id:
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Crystal structure of an anti-interleukin-2 monoclonal antibody Fab complexed with an antigenic nonapeptide.
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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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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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R.M.Cardoso,
M.B.Zwick,
R.L.Stanfield,
R.Kunert,
J.M.Binley,
H.Katinger,
D.R.Burton,
and
I.A.Wilson
(2005).
Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41.
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Immunity,
22,
163-173.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
