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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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PDB id:
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Immune system/hydrolase
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Title:
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Crystal structure of human angiogenin in complex with fab fragment of its monoclonal antibody mab 26-2f
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Structure:
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Antibody fab fragment, light chain. Chain: a. Engineered: yes. Other_details: hinge region observed in the fab fragment. Antibody fab fragment, heavy chain. Chain: b. Engineered: yes. Other_details: hinge region observed in the fab fragment. Angiogenin.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
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Biol. unit:
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Trimer (from PDB file)
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Resolution:
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2.00Å
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R-factor:
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0.232
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R-free:
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0.272
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Authors:
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G.B.Chavali,A.C.Papageorgiou,K.R.Acharya
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Key ref:
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G.B.Chavali
et al.
(2003).
The crystal structure of human angiogenin in complex with an antitumor neutralizing antibody.
Structure,
11,
875-885.
PubMed id:
DOI:
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Date:
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19-Jun-02
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Release date:
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19-Jun-03
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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DOI no:
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Structure
11:875-885
(2003)
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PubMed id:
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The crystal structure of human angiogenin in complex with an antitumor neutralizing antibody.
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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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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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Selected figure(s)
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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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Figure was
selected
by the author.
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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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G.Scarabelli,
G.Morra,
and
G.Colombo
(2010).
Predicting interaction sites from the energetics of isolated proteins: a new approach to epitope mapping.
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Biophys J,
98,
1966-1975.
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S.Li,
and
G.F.Hu
(2010).
Angiogenin-mediated rRNA transcription in cancer and neurodegeneration.
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Int J Biochem Mol Biol,
1,
26-35.
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D.M.Monti,
W.Yu,
E.Pizzo,
K.Shima,
M.G.Hu,
C.Di Malta,
R.Piccoli,
G.D'Alessio,
and
G.F.Hu
(2009).
Characterization of the angiogenic activity of zebrafish ribonucleases.
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FEBS J,
276,
4077-4090.
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N.Krauss,
H.Wessner,
K.Welfle,
H.Welfle,
C.Scholz,
M.Seifert,
K.Zubow,
J.Aÿ,
M.Hahn,
P.Scheerer,
A.Skerra,
and
W.Höhne
(2008).
The structure of the anti-c-myc antibody 9E10 Fab fragment/epitope peptide complex reveals a novel binding mode dominated by the heavy chain hypervariable loops.
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Proteins,
73,
552-565.
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PDB codes:
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D.Wu,
W.Yu,
H.Kishikawa,
R.D.Folkerth,
A.J.Iafrate,
Y.Shen,
W.Xin,
K.Sims,
and
G.F.Hu
(2007).
Angiogenin loss-of-function mutations in amyotrophic lateral sclerosis.
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Ann Neurol,
62,
609-617.
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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
codes are
shown on the right.
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Links
