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PDBsum entry 2ofc
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Sugar binding protein
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PDB id
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2ofc
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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 basis for the carbohydrate recognition of the sclerotium rolfsii lectin.
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Authors
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D.D.Leonidas,
B.M.Swamy,
G.N.Hatzopoulos,
S.J.Gonchigar,
V.B.Chachadi,
S.R.Inamdar,
S.E.Zographos,
N.G.Oikonomakos.
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Ref.
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J Mol Biol, 2007,
368,
1145-1161.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of a novel fungal lectin from Sclerotium rolfsii (SRL) in
its free form and in complex with N-acetyl-d-galactosamine (GalNAc) and
N-acetyl- d -glucosamine (GlcNAc) has been determined at 1.1 A, 2.0 A, and 1.7 A
resolution, respectively. The protein structure is composed of two beta-sheets,
which consist of four and six beta-strands, connected by two alpha-helices.
Sequence and structural comparisons reveal that SRL is the third member of a
newly identified family of fungal lectins, which includes lectins from Agaricus
bisporus and Xerocomus chrysenteron that share a high degree of structural
similarity and carbohydrate specificity. The data for the free SRL are the
highest resolution data for any protein of this family. The crystal structures
of the SRL in complex with two carbohydrates, GalNAc and GlcNAc, which differ
only in the configuration of a single epimeric hydroxyl group, provide the
structural basis for its carbohydrate specificity. SRL has two distinct
carbohydrate-binding sites, a primary and a secondary. GalNAc binds at the
primary site, whereas GlcNAc binds only at the secondary site. Thus, SRL has the
ability to recognize and probably bind at the same time two different
carbohydrate structures. Structural comparison to Agaricus bisporus
lectin-carbohydrate complexes reveals that the primary site is also able to bind
the Thomsen-Friedenreich antigen (Galbeta1-->3GalNAc-alpha- glycan structures)
whereas the secondary site cannot. The features of the molecular recognition at
the two sites are described in detail.
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Figure 2.
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Figure 7.
Figure 7. Stereo view of the superposition of the C^α traces
of the SRL (grey), ABL (red) and XCL (green) monomers.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2007,
368,
1145-1161)
copyright 2007.
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