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* Residue conservation analysis
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DOI no:
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EMBO J
16:5162-5177
(1997)
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PubMed id:
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Molecular recognition of human angiogenin by placental ribonuclease inhibitor--an X-ray crystallographic study at 2.0 A resolution.
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A.C.Papageorgiou,
R.Shapiro,
K.R.Acharya.
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ABSTRACT
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Human placental RNase inhibitor (hRI), a leucine-rich repeat protein, binds the
blood vessel-inducing protein human angiogenin (Ang) with extraordinary affinity
(Ki <1 fM). Here we report a 2.0 A resolution crystal structure for the
hRI-Ang complex that, together with extensive mutagenesis data from earlier
studies, reveals the molecular features of this tight interaction. The hRI-Ang
binding interface is large and encompasses 26 residues from hRI and 24 from Ang,
recruited from multiple domains of both proteins. However, a substantial
fraction of the energetically important contacts involve only a single region of
each: the C-terminal segment 434-460 of hRI and the ribonucleolytic active
centre of Ang, most notably the catalytic residue Lys40. Although the overall
docking of Ang resembles that observed for RNase A in the crystal structure of
its complex with the porcine RNase inhibitor, the vast majority of the
interactions in the two complexes are distinctive, indicating that the broad
specificity of the inhibitor for pancreatic RNase superfamily proteins is based
largely on its capacity to recognize features unique to each of them. The
implications of these findings for the development of small, hRI-based
inhibitors of Ang for therapeutic use are discussed.
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Selected figure(s)
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Figure 4.
Figure 4 Stereo views of hRI (A) and Ang (B) (C^  atoms
plus side chains of contact residues), and hRI (thick lines,
upper case letters) plus Ang (thin lines, lower case letters)
together (contact residues only) (C) in the hRI -Ang complex.
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Figure 5.
Figure 5 (A -E) Detailed interactions at the hRI -Ang interface.
hRI residues have filled bonds; Ang residues have empty bonds.
Drawn with the program MOLSCRIPT (Kraulis, 1991).
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(1997,
16,
5162-5177)
copyright 1997.
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Figures were
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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PDB code:
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