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PDBsum entry 1jb3
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Cell adhesion
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PDB id
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1jb3
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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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The laminin-Binding domain of agrin is structurally related to n-Timp-1.
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Authors
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J.Stetefeld,
M.Jenny,
T.Schulthess,
R.Landwehr,
B.Schumacher,
S.Frank,
M.A.Rüegg,
J.Engel,
R.A.Kammerer.
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Ref.
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Nat Struct Biol, 2001,
8,
705-709.
[DOI no: ]
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PubMed id
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Abstract
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Agrin is the key organizer of postsynaptic differentiation at the neuromuscular
junction. This organization activity requires the binding of agrin to the
synaptic basal lamina. Binding is conferred by the N-terminal agrin (NtA)
domain, which mediates a high-affinity interaction with the coiled coil domain
of laminins. Here, we report the crystal structure of chicken NtA at 1.6 A
resolution. The structure reveals that NtA harbors an
oligosaccharide/oligonucleotide-binding fold with several possible sites for the
interaction with different ligands. A high structural similarity of NtA with the
protease inhibition domain in tissue inhibitor of metalloproteinases-1 (TIMP-1)
supports the idea of additional functions of agrin besides synaptogenic activity.
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Figure 3.
Figure 3. Stereo view of the section of the final 2.7 Å
resolution 2F[o] - F[c] electron density map (blue; 1  contour
level) around the N-terminal segment of the NtA structure in
complex (starting with Cys 2). The chloride ion (red sphere)
is trapped between Arg 5 and Ser 108. The free model of NtA in
green (starting with Glu 6) is superimposed. Other than the
rigidification of their N-terminal tail regions, the free and
complexed structures are identical (overall r.m.s. deviation of
0.32 Å).
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Figure 4.
Figure 4. Electrostatic surface representation of the complexed
NtA domain. a, Front view of the structure. N- and C-termini
are to the left as in Fig. 1a. b, Back view of the NtA domain
domain related to the representation in (a) rotated by 120°
around the vertical axis. The molecular surface is shown in
white, and negatively and positively charged side chains are
colored red and blue, respectively.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2001,
8,
705-709)
copyright 2001.
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