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PDBsum entry 1dwz
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Prion protein
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PDB id
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1dwz
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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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Nmr structure of the bovine prion protein.
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Authors
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F.López garcia,
R.Zahn,
R.Riek,
K.Wüthrich.
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Ref.
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Proc Natl Acad Sci U S A, 2000,
97,
8334-8339.
[DOI no: ]
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PubMed id
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Abstract
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The NMR structures of the recombinant 217-residue polypeptide chain of the
mature bovine prion protein, bPrP(23-230), and a C-terminal fragment,
bPrP(121-230), include a globular domain extending from residue 125 to residue
227, a short flexible chain end of residues 228-230, and an N-terminal flexibly
disordered "tail" comprising 108 residues for the intact protein and 4 residues
for bPrP(121-230), respectively. The globular domain contains three
alpha-helices comprising the residues 144-154, 173-194, and 200-226, and a short
antiparallel beta-sheet comprising the residues 128-131 and 161-164. The
best-defined parts of the globular domain are the central portions of the
helices 2 and 3, which are linked by the only disulfide bond in bPrP.
Significantly increased disorder and mobility is observed for helix 1, the loop
166-172 leading from the beta-strand 2 to helix 2, the end of helix 2 and the
following loop, and the last turn of helix 3. Although there are characteristic
local differences relative to the conformations of the murine and Syrian hamster
prion proteins, the bPrP structure is essentially identical to that of the human
prion protein. On the other hand, there are differences between bovine and human
PrP in the surface distribution of electrostatic charges, which then appears to
be the principal structural feature of the "healthy" PrP form that might affect
the stringency of the species barrier for transmission of prion diseases between
humans and cattle.
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Figure 1.
Fig. 1. (a) Cartoon of the three-dimensional structure of
the intact bPrP(23-230). Helices are green,  -strands are
cyan, segments with nonregular secondary structure within the
C-terminal domain are yellow, and the flexibly disordered "tail"
of residues 23-121 is represented by 108 yellow dots, each of
which represents a residue of the tail (the numeration for hPrP
is used, and the insertions and deletions are placed according
to the alignment in ref. 23). (b) Stereo-view of an all-heavy
atom presentation of the globular domain in bPrP(23-230), with
residues 121-230, in the same orientation as in a. The backbone
is shown as a green spline function through the C^  positions,
hydrophobic side chains are yellow, and polar and charged side
chains are violet. (c and d) Surface views of the globular
domains of bPrP and hPrP, respectively. The orientation of the
molecule is slightly changed relative to a, so that the residue
186 is approximately in the center. The electrostatic surface
potential is indicated in red (negative charge), white
(neutral), and blue (positive charge). The figures were prepared
with the program MOLMOL (42).
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Figure 5.
Fig. 5. Data characterizing the internal mobility of the
globular domain of bPrP. (a) Steady-state 15N{1H}-NOEs of
bPrP(121-230), where Leu-125 is the first residue with a
positive NOE. (b) Longitudinal 15N spin-relaxation times,
T[1](15N). (c) Transverse 15N spin-relaxation times, T[2](15N).
The arrow indicates an upper limit for T[2](15N) of the residues
166-172. The locations of the regular secondary structure
elements are indicated in a.
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