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PDBsum entry 1vex
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Cell adhesion
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PDB id
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1vex
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References listed in PDB file
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Key reference
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Title
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Solution structures of the first and fourth tsr domains of f-Spondin.
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Authors
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K.Pääkkönen,
H.Tossavainen,
P.Permi,
H.Rakkolainen,
H.Rauvala,
E.Raulo,
I.Kilpeläinen,
P.Güntert.
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Ref.
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Proteins, 2006,
64,
665-672.
[DOI no: ]
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PubMed id
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Abstract
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F-spondin is a protein mainly associated with neuronal development. It attaches
to the extracellular matrix and acts in the axon guidance of the developing
nervous system. F-spondin consists of eight domains, six of which are TSR
domains. The TSR domain family binds a wide range of targets. Here we present
the NMR solution structures of TSR1 and TSR4. TSR domains have an unusual fold
that is characterized by a long, nonglobular shape, consisting of two
beta-strands and one irregular extended strand. Three disulfide bridges and
stack of alternating tryptophan and arginine side-chains stabilize the
structure. TSR1 and TSR4 structures are similar to each other and to the
previously determined TSR domain X-ray structures from another protein, TSP,
although TSR4 exhibits a mobile loop not seen in other structures.
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Figure 1.
Figure 1. The NMR solution of structures of (A) the F-spondin
TSR domain 1 and (B) the F-spondin TSR domain 4. Twenty
energy-refined conformers are shown for each domain. The first
strand has a rippled conformation, which is characteristic for
this fold. The two other strands form an antiparallel  -sheet
(residues 462-467 and 484-489 for TSR1, and 634-640 and 657-663
for TSR4). TSR1 has a short additional -sheet
in the region where TSR4 has a less well-defined loop region
(residues 443-445 and 471-473). The secondary structure and core
residues of a representative conformer of the solution
structures of the F-spondin (C) TSR1 and (D) TSR4 domains are
shown. Tryptophans are drawn in blue, arginines in red, and
cysteines in yellow. The green residue in TSR1 is tyrosine,
which may further stabilize the structure through interactions
with the nearby arginine side-chain. In TSR4, this residue is
leucine. Aspartate 485 is shown in magenta.
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Figure 4.
Figure 4. Electrostatic surface potentials of (A) TSP TSR2, (B)
F-spondin TSR1, and (C) F-spondin TSR4. Each domain is shown
from two sides, which are rotated by 180° around a vertical
axis relative to each other. For the F-spondin TSR domains, the
structures with the lowest total energy are shown. Charged
residues are labeled. Red labels identify residues that are
conserved in the sequence alignment and have similar positions
on the surfaces of all three domains. The charged side-chains
D496, E497, and D498 in F-spondin TSR1 and D625, K632, K642,
E646, D649, and D653 in F-spondin TSR4 have larger than 2
Å side-chain RMSDs.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2006,
64,
665-672)
copyright 2006.
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