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PDBsum entry 1h4u
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Extracellular matrix protein
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PDB id
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1h4u
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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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Crystal structure and mutational analysis of a perlecan-Binding fragment of nidogen-1.
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Authors
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M.Hopf,
W.Göhring,
A.Ries,
R.Timpl,
E.Hohenester.
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Ref.
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Nat Struct Biol, 2001,
8,
634-640.
[DOI no: ]
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PubMed id
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Abstract
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Nidogen, an invariant component of basement membranes, is a multifunctional
protein that interacts with most other major basement membrane proteins. Here,
we report the crystal structure of the mouse nidogen-1 G2 fragment, which
contains binding sites for collagen IV and perlecan. The structure is composed
of an EGF-like domain and an 11-stranded beta-barrel with a central helix. The
beta-barrel domain has unexpected similarity to green fluorescent protein. A
large surface patch on the beta-barrel is strikingly conserved in all metazoan
nidogens. Site-directed mutagenesis demonstrates that the conserved residues are
involved in perlecan binding.
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Figure 1.
Figure 1. The nidogen G2 structure. a, Stereo view of the
structure with the EGF-like domain in green and the  -barrel
domain in cyan. -strands
are labeled a -b in the EGF-like domain and A -K in the -barrel
domain. The  -helices
1 -3 are in red and disulfide bridges in yellow. To facilitate
the tracing of the polypeptide chain disordered segments
(residues 357 -366, 374 -380, 565 -570 and 588 -595) have been
included in arbitrary but stereochemically sensible
conformations and are shown in light gray. b, Topology diagram
of the -barrel
domain. The barrel is closed by the parallel interaction of
strands A and F. c, Stereo view of a portion of the experimental
electron density map after solvent flattening at 2.8 Å
resolution. The final model is superimposed on the map. Shown
are -strands
D, E and F. Figs 1a,c, 2 and 4 were made with BOBSCRIPT35 and
RASTER3D^36.
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Figure 2.
Figure 2. Comparison of the  -barrels
of nidogen G2 and Aequora victoria GFP22. Nidogen G2 is in
magenta and GFP in green. A total of 195 C atoms
were superimposed with an r.m.s. deviation of 2.5 Å. In the
nidogen G2 trace every 20^th C atom
is shown as a small, labeled sphere. The chromophore in GFP is
shown as a ball-and-stick model.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2001,
8,
634-640)
copyright 2001.
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Secondary reference #1
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Title
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Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV.
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Authors
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J.W.Fox,
U.Mayer,
R.Nischt,
M.Aumailley,
D.Reinhardt,
H.Wiedemann,
K.Mann,
R.Timpl,
T.Krieg,
J.Engel.
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Ref.
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Embo J, 1991,
10,
3137-3146.
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PubMed id
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