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PDBsum entry 1dfj
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Complex (endonuclease/inhibitor)
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PDB id
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1dfj
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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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A structural basis of the interactions between leucine-Rich repeats and protein ligands.
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Authors
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B.Kobe,
J.Deisenhofer.
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Ref.
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Nature, 1995,
374,
183-186.
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PubMed id
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Abstract
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The leucine-rich repeat is a recently characterized structural motif used in
molecular recognition processes as diverse as signal transduction, cell
adhesion, cell development, DNA repair and RNA processing. We present here the
crystal structure at 2.5 A resolution of the complex between ribonuclease A and
ribonuclease inhibitor, a protein built entirely of leucine-rich repeats. The
unusual non-globular structure of ribonuclease inhibitor, its solvent-exposed
parallel beta-sheet and the conformational flexibility of the structure are used
in the interaction; they appear to be the principal reasons for the
effectiveness of leucine-rich repeats as protein-binding motifs. The structure
can serve as a model for the interactions of other proteins containing
leucine-rich repeats with their ligands.
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Secondary reference #1
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Title
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Mechanism of ribonuclease inhibition by ribonuclease inhibitor protein based on the crystal structure of its complex with ribonuclease a.
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Authors
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B.Kobe,
J.Deisenhofer.
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Ref.
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J Mol Biol, 1996,
264,
1028-1043.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Figure 3.
Figure 3. Conformational changes
in RI. The models of RI from the
RNase A-RI complex (continuous
lines) and RI from the lithium
sulfate crystals (broken lines) were
superimposed on the high-resol-
ution model of free RI with the
program INSIGHT (using only the
C
a
atoms). The r.m.s. deviations of
the C
a
atoms are shown as thin
lines, and the fourth-order poly-
nomial curves fitted to the r.m.s.
deviations curves are shown as
thick lines.
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Figure 4.
Figure 4. An annealed omit electron density in the active site of RNase A. An 8 Å sphere around the sulfate ion
in the RNase active site was omitted and the immediate surrounding atoms consisting of a 3 Å shell were restrained
to avoid artificial movement into the omitted region. Simulated annealing was run with a starting temperature of
1000 Å . The stereo view of the electron density calculated with the phases derived from the omitted model and
coefficients =Fobs= - =Fcalc= for data between 40 and 2.5 Å , was contoured at 3s and plotted with a program written by
D. Xia. Superimposed is the model of the RNase A-RI complex. RNase A residues are indicated with E, and RI residues
are indicated with I.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #2
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Title
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Complex between bovine ribonuclease a and porcine ribonuclease inhibitor crystallizes in a similar unit cell as free ribonuclease inhibitor.
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Authors
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B.Kobe,
Z.Ma,
J.Deisenhofer.
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Ref.
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J Mol Biol, 1994,
241,
288-291.
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PubMed id
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