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PDBsum entry 2jvf
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De novo protein
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PDB id
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2jvf
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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 nmr solution structure of the artificial protein m7 matches the computationally designed model.
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Authors
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C.Stordeur,
R.Dallüge,
O.Birkenmeier,
H.Wienk,
R.Rudolph,
C.Lange,
C.Lücke.
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Ref.
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Proteins, 2008,
72,
1104-1107.
[DOI no: ]
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PubMed id
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Abstract
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No abstract given.
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Figure 1.
Figure 1. (A) Alignment of the protein sequences of M7 and
TOP7. Residues identical to the sequence of TOP7 are shaded in
green. Secondary structure elements of M7 are indicated above
the line as  -helix
( ),
 -strand
( ),
regular -turn
(t) or loop (l). Blue triangles mark the position of residues
with greater than 40% occluded surface in TOP7.[7] (B) Ribbon
diagram highlighting the secondary structure elements of the M7
solution structure. The five antiparallel -strands
(A-E) are indicated as cyan arrows, while the two -helices
(I and II) are shown in red/yellow. (C) Backbone trace
superposition of the final 20 energy-minimized M7 conformers
(yellow lines) with the designed structural model (magenta
ribbon).
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The above figure is
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
72,
1104-1107)
copyright 2008.
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Secondary reference #1
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Title
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A tetrapeptide fragment-Based design method results in highly stable artificial proteins.
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Authors
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R.Dallüge,
J.Oschmann,
O.Birkenmeier,
C.Lücke,
H.Lilie,
R.Rudolph,
C.Lange.
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Ref.
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Proteins, 2007,
68,
839-849.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2. Cartoon representation (A) and backbone conformation
(B) of the target structure. Atomic coordinates for the
representation were taken from the structure of TOP 7[7]
deposited in the pdb database (1QYS). The images were generated
using PyMol version 0.96 (DeLano Scientific, San Carlos, CA).
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Figure 3.
Figure 3. Alignment of the designed protein sequences M1
through M8 with TOP 7 (Kuhlman et al., 2003). Residues identical
to the sequence of TOP 7 are shaded in dark gray. Predefined
residues appear in black. Target conformational regions for the
 [2]/
 [3]
pairs are indicated above the respective second amino acids of
each tetrapeptide section. h: helix/   -turn,
e: -sheet/extended,
l: left-handed helix, and x: II -turn.
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The above figures are
reproduced from the cited reference
with permission from John Wiley & Sons, Inc.
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