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PDBsum entry 1h6u
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Cell adhesion
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PDB id
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1h6u
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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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Internalins from the human pathogen listeria monocytogenes combine three distinct folds into a contiguous internalin domain.
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Authors
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W.D.Schubert,
G.Göbel,
M.Diepholz,
A.Darji,
D.Kloer,
T.Hain,
T.Chakraborty,
J.Wehland,
E.Domann,
D.W.Heinz.
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Ref.
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J Mol Biol, 2001,
312,
783-794.
[DOI no: ]
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PubMed id
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Abstract
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Listeria monocytogenes is an opportunistic, food-borne human and animal
pathogen. Host cell invasion requires the action of the internalins A (InlA) and
B (InlB), which are members of a family of listerial cell-surface proteins.
Common to these proteins are three distinctive N-terminal domains that have been
shown to direct host cell-specific invasion for InlA and InlB. Here, we present
the high-resolution crystal structures of these domains present in InlB and
InlH, and show that they constitute a single "internalin domain". In
this internalin domain, a central LRR region is flanked contiguously by a
truncated EF-hand-like cap and an immunoglobulin (Ig)-like fold. The extended
beta-sheet, resulting from the distinctive fusion of the LRR and the Ig-like
folds, constitutes an adaptable concave interaction surface, which we propose is
responsible for the specific recognition of the host cellular binding partners
during infection.
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Figure 4.
Figure 4. Structure of a single LRR comprising 22 residues.
b-Strand and 3[10]-helix are indicated in red and blue,
respectively. Side-chain bonds of hydrophobic core residues are
shown and labeled in yellow. Exposed residue bonds are shaded
gray, while conserved and variable residue positions are labeled
in red and black, respectively.[55]
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Figure 8.
Figure 8. The continuous hydrophobic core of the internalin
domain in InlH[36-343]. The sub-domain colors correspond to
Figure 1. The molecular surface is cut away to reveal the
interior of the molecule. Hydrophobic amino acid side-chain
atoms in the core are shown in yellow. [57]
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2001,
312,
783-794)
copyright 2001.
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