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PDBsum entry 1qos
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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 basis of carbohydrate recognition by lectin ii from ulex europaeus, A protein with a promiscuous carbohydrate-Binding site.
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Authors
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R.Loris,
H.De greve,
M.H.Dao-Thi,
J.Messens,
A.Imberty,
L.Wyns.
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Ref.
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J Mol Biol, 2000,
301,
987.
[DOI no: ]
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PubMed id
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Abstract
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Protein-carbohydrate interactions are the language of choice for inter- cellular
communication. The legume lectins form a large family of homologous proteins
that exhibit a wide variety of carbohydrate specificities. The legume lectin
family is therefore highly suitable as a model system to study the structural
principles of protein-carbohydrate recognition. Until now, structural data are
only available for two specificity families: Man/Glc and Gal/GalNAc. No
structural data are available for any of the fucose or chitobiose specific
lectins.The crystal structure of Ulex europaeus (UEA-II) is the first of a
legume lectin belonging to the chitobiose specificity group. The complexes with
N-acetylglucosamine, galactose and fucosylgalactose show a promiscuous primary
binding site capable of accommodating both N-acetylglucos amine or galactose in
the primary binding site. The hydrogen bonding network in these complexes can be
considered suboptimal, in agreement with the low affinities of these sugars. In
the complexes with chitobiose, lactose and fucosyllactose this suboptimal
hydrogen bonding network is compensated by extensive hydrophobic interactions in
a Glc/GlcNAc binding subsite. UEA-II thus forms the first example of a legume
lectin with a promiscuous binding site and illustrates the importance of
hydrophobic interactions in protein-carbohydrate complexes. Together with other
known legume lectin crystal structures, it shows how different specificities can
be grafted upon a conserved structural framework.
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Figure 3.
Figure 3. Comparison of the tetramer formed by UEA-II and
DBL. (a) Ribbon diagram of the UEA-II tetramer. (b) Ribbon
diagram of the DBL tetramer showing the C-terminal helix in red.
(c) Close-up of the DB58-like interface of UEA-II showing the
disulphide linkage between Cys184 of two adjacent monomers. The
side-chains of Asp169, Val171, Thr173 and Arg175 (upper strand),
Ser180 Thr182, Cys184 and Ser186 (middle strand) and Ser193,
Ile195 and Thr197 (lower strand) are shown in ball-and-stick
representation. Cys184 is labelled. (d) Similar view of the
DB58-like interface of the DBL tetramer. The side-chains of
Glu163, Leu165, Thr167 and Asn169 (upper strand), Leu174,
Val176, Ser178 and Val180 (middle strand) and Ser187, Ile189 and
Ser191 (lower strand) are shown in ball-and-stick
representation. Ser178 (the equivalent of Cys184 in UEA-II) is
labelled.
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Figure 7.
Figure 7. Schematic drawing of oligosaccharide recognition
by UEA-II. (a) Binding of GlcNAc and chitobiose. (b) Binding of
galactose, lactose, fucosylgalactose and fucosyllactose.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2000,
301,
987-0)
copyright 2000.
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Secondary reference #1
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Title
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Novel structures of plant lectins and their complexes with carbohydrates.
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Authors
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J.Bouckaert,
T.Hamelryck,
L.Wyns,
R.Loris.
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Ref.
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Curr Opin Struct Biol, 1999,
9,
572-577.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Quaternary structure of uea-Ii, The chitobiose specific lectin from gorse.
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Authors
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M.H.Dao-Thi,
P.Rizkallah,
L.Wyns,
F.Poortmans,
R.Loris.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1998,
54,
844-847.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. (a) 1
° rotation picture taken at station 7.2 of the Daresbury
synchrotron. The crystal is oriented with its c* axis approximately
parallel to the camera axis around which the crystal was rotated
during the exposure. (b) Enlargement of a portion of the diffraction
pattern showing diffraction at the edge of the image (2.7 A).
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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Secondary reference #3
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Title
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Legume lectin structure.
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Authors
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R.Loris,
T.Hamelryck,
J.Bouckaert,
L.Wyns.
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Ref.
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Biochim Biophys Acta, 1998,
1383,
9.
[DOI no: ]
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PubMed id
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