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PDBsum entry 1h0d
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Immune system/hydrolase
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PDB id
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1h0d
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Contents |
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216 a.a.
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223 a.a.
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123 a.a.
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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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The crystal structure of human angiogenin in complex with an antitumor neutralizing antibody.
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Authors
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G.B.Chavali,
A.C.Papageorgiou,
K.A.Olson,
J.W.Fett,
G.Hu,
R.Shapiro,
K.R.Acharya.
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Ref.
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Structure, 2003,
11,
875-885.
[DOI no: ]
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PubMed id
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Abstract
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The murine monoclonal antibody 26-2F neutralizes the angiogenic and
ribonucleolytic activities of human angiogenin (ANG) and is highly effective in
preventing the establishment and metastatic dissemination of human tumors in
athymic mice. Here we report a 2.0 A resolution crystal structure for the
complex of ANG with the Fab fragment of 26-2F that reveals the detailed
interactions between ANG and the complementarity-determining regions (CDRs) of
the antibody. Surprisingly, Fab binding induces a dramatic conformational change
in the cell binding region of ANG at the opposite end of the molecule from the
combining site; crosslinking experiments indicate that this rearrangement also
occurs in solution. The ANG-Fab complex structure should be invaluable for
designing maximally humanized versions of 26-2F for potential clinical use.
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Figure 1.
Figure 1. Structure of the Complex Formed between Human ANG
and Fab 26-2FThe L and H chains of the Fab molecule are in
magenta and blue, respectively, except for their CDRs (L1-L3 and
H1-H3), which are in gold and cyan, respectively. ANG, green.
Sulfate ions (yellow bonds) and glycerol molecules (green bonds)
are also shown. The figure was generated with MOLSCRIPT
(Kraulis, 1991).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
875-885)
copyright 2003.
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