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* Residue conservation analysis
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DOI no:
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EMBO J
20:5342-5346
(2001)
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PubMed id:
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Structural basis for the high-affinity interaction of nidogen-1 with immunoglobulin-like domain 3 of perlecan.
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M.Kvansakul,
M.Hopf,
A.Ries,
R.Timpl,
E.Hohenester.
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ABSTRACT
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Nidogen and perlecan are large multifunctional basement membrane (BM) proteins
conserved in all metazoa. Their high-affinity interaction, which is likely to
contribute to BM assembly and function, is mediated by the central G2 domain in
nidogen and the third immunoglobulin (IG)-like domain in perlecan, IG3. We have
solved the crystal structure at 2.0 A resolution of the mouse nidogen-1
G2-perlecan IG3 complex. Perlecan IG3 belongs to the I-set of the IG superfamily
and binds to the wall of the nidogen-1 G2 beta-barrel using beta-strands C, D
and F. Nidogen-1 residues participating in the extensive interface are highly
conserved, whereas the corresponding binding site on perlecan is more variable.
We hypothesize that a second, as yet unidentified, activity of nidogen overlaps
with perlecan binding and accounts for the unusually high degree of surface
conservation in the G2 domain.
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Selected figure(s)
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Figure 1.
Figure 1 Domain organization of mouse perlecan (Noonan et al.,
1991) and nidogen-1 (Mann et al., 1989). HS, heparan sulfate
oligosaccharide chains; SEA, domain found in sea urchin sperm
protein, enterokinase, agrin; LA, LDL receptor type A; IG,
immunoglobulin-like; L4, laminin domain IV; LE, laminin type
epidermal growth factor-like; LG, laminin G-like; EG, epidermal
growth factor-like; TY, thyroglobulin-like; G1 -3, nidogen
globular domains. The double-headed arrow indicates the
high-affinity interaction between nidogen-1 G2 (in cyan, with
the preceding EG domain in green) and perlecan IG3 (in magenta).
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Figure 3.
Figure 3 Stereoview of the nidogen-1 G2 -perlecan IG3 interface.
Nidogen-1 and perlecan residues are in cyan and magenta,
respectively, and are labelled, as are  -strands
contributing to the interface. Hydrogen bonds are indicated by
thin black lines. The view direction is similar to the lower
panel in Figure 2A.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2001,
20,
5342-5346)
copyright 2001.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.F.Gruber,
R.DeSalle,
E.K.Lienau,
D.Tchernov,
V.A.Pieribone,
and
H.T.Kao
(2009).
Novel internal regions of fluorescent proteins undergo divergent evolutionary patterns.
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Mol Biol Evol,
26,
2841-2848.
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P.Mendoza-Espinosa,
V.García-González,
A.Moreno,
R.Castillo,
and
J.Mas-Oliva
(2009).
Disorder-to-order conformational transitions in protein structure and its relationship to disease.
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Mol Cell Biochem,
330,
105-120.
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M.S.Ho,
K.Böse,
S.Mokkapati,
R.Nischt,
and
N.Smyth
(2008).
Nidogens-Extracellular matrix linker molecules.
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Microsc Res Tech,
71,
387-395.
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T.J.Mankelow,
N.Burton,
F.O.Stefansdottir,
F.A.Spring,
S.F.Parsons,
J.S.Pedersen,
C.L.Oliveira,
D.Lammie,
T.Wess,
N.Mohandas,
J.A.Chasis,
R.L.Brady,
and
D.J.Anstee
(2007).
The Laminin 511/521-binding site on the Lutheran blood group glycoprotein is located at the flexible junction of Ig domains 2 and 3.
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Blood,
110,
3398-3406.
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PDB codes:
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J.C.Jones,
K.Lane,
S.B.Hopkinson,
E.Lecuona,
R.C.Geiger,
D.A.Dean,
E.Correa-Meyer,
M.Gonzales,
K.Campbell,
J.I.Sznajder,
and
S.Budinger
(2005).
Laminin-6 assembles into multimolecular fibrillar complexes with perlecan and participates in mechanical-signal transduction via a dystroglycan-dependent, integrin-independent mechanism.
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J Cell Sci,
118,
2557-2566.
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I.Halperin,
H.Wolfson,
and
R.Nussinov
(2004).
Protein-protein interactions; coupling of structurally conserved residues and of hot spots across interfaces. Implications for docking.
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Structure,
12,
1027-1038.
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S.Hummel,
A.Osanger,
T.M.Bajari,
M.Balasubramani,
W.Halfter,
J.Nimpf,
and
W.J.Schneider
(2004).
Extracellular matrices of the avian ovarian follicle. Molecular characterization of chicken perlecan.
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J Biol Chem,
279,
23486-23494.
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T.Sasaki,
R.Fässler,
and
E.Hohenester
(2004).
Laminin: the crux of basement membrane assembly.
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J Cell Biol,
164,
959-963.
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R.Kalluri
(2003).
Basement membranes: structure, assembly and role in tumour angiogenesis.
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Nat Rev Cancer,
3,
422-433.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
