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PDBsum entry 1rdl
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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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Structural analysis of monosaccharide recognition by rat liver mannose-Binding protein.
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Authors
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K.K.Ng,
K.Drickamer,
W.I.Weis.
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Ref.
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J Biol Chem, 1996,
271,
663-674.
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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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The structural basis of carbohydrate recognition by rat liver mannose-binding
protein (MBP-C) has been explored by determining the three-dimensional structure
of the C-type carbohydrate-recognition domain (CRD) of MBP-C using x-ray
crystallography. The structure was solved by molecular replacement using rat
serum mannose-binding protein (MBP-A) as a search model and was refined to
maximum Bragg spacings of 1.7 A. Despite their almost identical folds, the
dimeric structures formed by the two MBP CRDs differ dramatically. Complexes of
MBP-C with methyl glycosides of mannose, N-acetylglucosamine, and fucose were
prepared by soaking MBP-C crystals in solutions containing these sugars.
Surprisingly, the pyranose ring of mannose is rotated 180 degrees relative to
the orientation observed previously in MBP-A, but the local interactions between
sugar and protein are preserved. For each of the bound sugars, vicinal,
equatorial hydroxyl groups equivalent to the 3- and 4-OH groups of mannose
directly coordinate Ca2+ and form hydrogen bonds with residues also serving as
Ca2+ ligands. Few interactions are observed between other parts of the sugar and
the protein. A complex formed between free galactose and MBP-C reveals a similar
mode of binding, with the anomeric hydroxyl group serving as one of the Ca2+
ligands. A second binding site for mannose has also been observed in one of two
copies in the asymmetric unit at a sugar concentration of 1.3 M. These
structures explain how MBPs recognize a wide range of monosaccharides and
suggest how fine specificity differences between MBP-A and MBP-C may be achieved.
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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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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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Secondary reference #3
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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 #4
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Title
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Differential recognition of core and terminal portions of oligosaccharide ligands by carbohydrate-Recognition domains of two mannose-Binding proteins.
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Authors
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R.A.Childs,
T.Feizi,
C.T.Yuen,
K.Drickamer,
M.S.Quesenberry.
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Ref.
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J Biol Chem, 1990,
265,
20770-20777.
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PubMed id
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