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PDBsum entry 1rtm
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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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Trimeric structure of a c-Type mannose-Binding protein.
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Authors
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W.I.Weis,
K.Drickamer.
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Ref.
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Structure, 1994,
2,
1227-1240.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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BACKGROUND: Mannose-binding proteins (MBPs) are C-type (Ca(2+)-dependent) animal
lectins found in serum. They recognize cell-surface oligosaccharide structures
characteristic of pathogenic bacteria and fungi, and trigger the neutralization
of these organisms. Like most lectins, MBPs display weak intrinsic affinity for
monovalent sugar ligands, but bind avidly to multivalent ligands. RESULTS: We
report physical studies in solution and the crystal structure determined at 1.8
A Bragg spacings of a trimeric fragment of MBP-A, containing the
carbohydrate-recognition domain (CRD) and the neck domain that links the
carboxy-terminal CRD to the collagen-like portion of the intact molecule. The
neck consists of a parallel triple-stranded coiled coil of alpha-helices linked
by four residues to the CRD. The isolated neck peptide does not form stable
helices in aqueous solution. The previously characterized carbohydrate-binding
sites lie at the distal end of the trimer and are separated from each other by
53 A. CONCLUSIONS: The carbohydrate-binding sites in MBP-A are too far apart for
a single trimer to bind multivalently to a typical mammalian high-mannose
oligosaccharide. Thus MBPs can recognize pathogens selectively by binding avidly
only to the widely spaced, repetitive sugar arrays on pathogenic cell surfaces.
Sequence alignments reveal that other C-type lectins are likely to have a
similar oligomeric structure, but differences in their detailed organization
will have an important role in determining their interactions with
oligosaccharides.
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Figure 7.
Figure 7. A portion of the neck–CRD interface, shown with the
1.25σ contour of the final 2F[o]–F[c] map. Conserved
hydrophobic residues are labeled; the residues come from the
protomer whose number precedes the amino acid name. Figure 7.
A portion of the neck–CRD interface, shown with the 1.25σ
contour of the final 2F[o]–F[c] map. Conserved hydrophobic
residues are labeled; the residues come from the protomer whose
number precedes the amino acid name.
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Figure 8.
Figure 8. Representative sequences of the neck region and
portions of the CRDs following the last Gly-X-Y repeat taken
from various subgroups of collectins. RA, rat; HU, human. The a
and d positions of the heptadrepeats are indicated. Sites of
introns and the sites of subtilisin digestion that releases the
carboxy-terminal CRDs of MBPs are underlined. Residues inthe
neck–CRD interface (see Table 2) are denoted with asterisks.
Sequences and intron positions are derived from [19, 44, 61, 62,
63, 64 and 65]. Figure 8. Representative sequences of the
neck region and portions of the CRDs following the last Gly-X-Y
repeat taken from various subgroups of collectins. RA, rat; HU,
human. The a and d positions of the heptadrepeats are indicated.
Sites of introns and the sites of subtilisin digestion that
releases the carboxy-terminal CRDs of MBPs are underlined.
Residues inthe neck–CRD interface (see [3]Table 2) are denoted
with asterisks. Sequences and intron positions are derived from
[[4]19, [5]44, [6]61, [7]62, [8]63, [9]64 and [10]65].
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The above figures are
reprinted
by permission from Cell Press:
Structure
(1994,
2,
1227-1240)
copyright 1994.
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Secondary reference #1
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Title
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Structure of a c-Type mannose-Binding protein complexed with an oligosaccharide.
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Authors
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W.I.Weis,
K.Drickamer,
W.A.Hendrickson.
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Ref.
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Nature, 1992,
360,
127-134.
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PubMed id
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Secondary reference #2
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Title
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Physical characterization and crystallization of the carbohydrate-Recognition domain of a mannose-Binding protein from rat.
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Authors
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W.I.Weis,
G.V.Crichlow,
H.M.Murthy,
W.A.Hendrickson,
K.Drickamer.
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Ref.
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J Biol Chem, 1991,
266,
20678-20686.
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PubMed id
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Secondary reference #3
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Title
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Structure of the calcium-Dependent lectin domain from a rat mannose-Binding protein determined by mad phasing.
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Authors
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W.I.Weis,
R.Kahn,
R.Fourme,
K.Drickamer,
W.A.Hendrickson.
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Ref.
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Science, 1991,
254,
1608-1615.
[DOI no: ]
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PubMed id
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