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PDBsum entry 1tle
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References listed in PDB file
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Key reference
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Title
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Structure of the nidogen binding le module of the laminin gamma1 chain in solution.
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Authors
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R.Baumgartner,
M.Czisch,
U.Mayer,
E.Pöschl,
R.Huber,
R.Timpl,
T.A.Holak.
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Ref.
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J Mol Biol, 1996,
257,
658-668.
[DOI no: ]
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PubMed id
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Abstract
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The structure of the single LE module between residues 791 and 848 of the
laminin gamma1 chain, which contains the high affinity binding site for nidogen,
has been probed using NMR methods. The module folds into an autonomous domain
which has a stable and unique three-dimensional (3D) structure in solution. The
3D structure was determined on the basis of 362 interproton distance constraints
derived from nuclear Overhauser enhancement measurements and 39 phi angles,
supplemented by 5 psi and 22 chi1 angles. The main features of the NMR
structures are two-stranded antiparallel beta-sheets which are separated by
loops and cross-connected by four disulfide bridges. The N-terminal segment
which contains the first three disulfide bridges is similar to epidermal growth
factor. The C-terminal segment has an S-like backbone profile with a crossover
at the last disulfide bridge and comprises two three-residue long beta-strands
that form an antiparallel beta-sheet. The LE module possesses an exposed nidogen
binding loop that projects away from the main body of the protein. The
side-chains of three amino acids which are crucial for binding (Asp, Asn, Val)
are all exposed at the domain surface. An inactivating Asn-Ser mutation in this
region showed the same 3D structure indicating that these three residues, and
possibly an additional Tyr in an adjacent loop, provide direct contacts in the
interaction with nidogen.
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Figure 9.
Figure 9. Best superposition of g1III4 module on the structure of mouse EGF. g1III4 is shown in green and EGF in
red (Kohda & Ihagaki, 1992).
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Figure 10.
Figure 10. Best superposition of the constrained energy minimized average structure (SA)m for g1III4 with the X-ray
structure (Stetefeld et al., 1996).
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1996,
257,
658-668)
copyright 1996.
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Secondary reference #1
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Title
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Two non-Contiguous regions contribute to nidogen binding to a single egf-Like motif of the laminin gamma 1 chain.
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Authors
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E.Pöschl,
J.W.Fox,
D.Block,
U.Mayer,
R.Timpl.
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Ref.
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Embo J, 1994,
13,
3741-3747.
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PubMed id
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Secondary reference #2
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Title
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A single egf-Like motif of laminin is responsible for high affinity nidogen binding.
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Authors
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U.Mayer,
R.Nischt,
E.Pöschl,
K.Mann,
K.Fukuda,
M.Gerl,
Y.Yamada,
R.Timpl.
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Ref.
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Embo J, 1993,
12,
1879-1885.
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PubMed id
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