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PDBsum entry 1hlc
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Contents |
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* Residue conservation analysis
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PDB id:
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Lectin
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Title:
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X-ray crystal structure of the human dimeric s-lac lectin, l-14-ii, in complex with lactose at 2.9 angstroms resolution
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Structure:
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Human lectin. Chain: a, b. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: cdna
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Biol. unit:
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Dimer (from
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Resolution:
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Authors:
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Y.D.Lobsanov,M.A.Gitt,H.Leffler,S.Barondes,J.M.Rini
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Key ref:
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Y.D.Lobsanov
et al.
(1993).
X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.
J Biol Chem,
268,
27034-27038.
PubMed id:
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Date:
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13-Oct-93
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Release date:
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30-Apr-94
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PROCHECK
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Headers
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References
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P05162
(LEG2_HUMAN) -
Galectin-2 from Homo sapiens
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Seq:
Struc:
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132 a.a.
129 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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J Biol Chem
268:27034-27038
(1993)
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PubMed id:
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X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.
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Y.D.Lobsanov,
M.A.Gitt,
H.Leffler,
S.H.Barondes,
J.M.Rini.
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ABSTRACT
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S-Lac lectins are a family of soluble lactose-binding animal lectins, some of
which have been implicated in modulating cell-cell and cell-matrix interactions
through specific carbohydrate-mediated recognition. We report here the x-ray
crystal structure of a representative member of this family, the human dimeric
S-Lac lectin, L-14-II, in complex with lactose, at 2.9-A resolution. The
two-fold symmetric dimer is made up of two extended anti-parallel beta-sheets,
which associate in a beta-sandwich motif. Remarkably, the L-14-II monomer shares
not only the same topology, but a very similar beta-sheet structure with that of
the leguminous plant lectins, suggesting a conserved structure-function
relationship. Carbohydrate binding by L-14-II was found to involve protein
residues that are very highly conserved among all S-Lac lectins. These residues
map to a single DNA exon, suggesting a carbohydrate binding cassette common to
all S-Lac lectins.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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B.Lyimo,
F.Yagi,
and
Y.Minami
(2011).
Primary structure and specificity of a new member of galectin family from the Amethyst deceiver mushroom Laccaria amethystina.
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Biosci Biotechnol Biochem,
75,
62-69.
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K.Nishiyama,
A.Yamada,
M.Takahashi,
T.Takeuchi,
K.Kasai,
S.Kobayashi,
H.Natsugari,
and
H.Takahashi
(2010).
Synthesis of fluorescence-labeled Galbeta1-3Fuc and Galbeta1-4Fuc as probes for the endogenous glyco-epitope recognized by galectins in Caenorhabditis elegans.
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Chem Pharm Bull (Tokyo),
58,
495-500.
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G.R.Vasta
(2009).
Roles of galectins in infection.
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Nat Rev Microbiol,
7,
424-438.
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R.D.Cummings
(2009).
The repertoire of glycan determinants in the human glycome.
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Mol Biosyst,
5,
1087-1104.
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T.Takeuchi,
K.Nishiyama,
K.Sugiura,
M.Takahashi,
A.Yamada,
S.Kobayashi,
H.Takahashi,
H.Natsugari,
and
K.Kasai
(2009).
Caenorhabditis elegans galectins LEC-6 and LEC-1 recognize a chemically synthesized Galbeta1-4Fuc disaccharide unit which is present in Protostomia glycoconjugates.
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Glycobiology,
19,
1503-1510.
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Y.Nemoto-Sasaki,
and
K.Kasai
(2009).
Deletion of lec-10, a galectin-encoding gene, increases susceptibility to oxidative stress in Caenorhabditis elegans.
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Biol Pharm Bull,
32,
1973-1977.
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D.Houzelstein,
I.R.Gonçalves,
A.Orth,
F.Bonhomme,
and
P.Netter
(2008).
Lgals6, a 2-million-year-old gene in mice: a case of positive Darwinian selection and presence/absence polymorphism.
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Genetics,
178,
1533-1545.
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D.Zhou,
H.Ge,
J.Sun,
Y.Gao,
M.Teng,
and
L.Niu
(2008).
Crystal structure of the C-terminal conserved domain of human GRP, a galectin-related protein, reveals a function mode different from those of galectins.
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Proteins,
71,
1582-1588.
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PDB code:
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E.M.Rapoport,
O.V.Kurmyshkina,
and
N.V.Bovin
(2008).
Mammalian galectins: structure, carbohydrate specificity, and functions.
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Biochemistry (Mosc),
73,
393-405.
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M.A.Wälti,
S.Thore,
M.Aebi,
and
M.Künzler
(2008).
Crystal structure of the putative carbohydrate recognition domain of human galectin-related protein.
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Proteins,
72,
804-808.
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PDB code:
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M.Tamura,
K.Kasai,
T.Itagaki,
T.Nonaka,
and
Y.Arata
(2008).
Identification of a second, non-conserved amino acid that contributes to the unique sugar binding properties of the nematode galectin LEC-1.
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Biol Pharm Bull,
31,
1254-1257.
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S.R.Stowell,
C.M.Arthur,
K.A.Slanina,
J.R.Horton,
D.F.Smith,
and
R.D.Cummings
(2008).
Dimeric Galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain.
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J Biol Chem,
283,
20547-20559.
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Y.Arata,
N.Ishii,
M.Tamura,
T.Nonaka,
and
K.Kasai
(2007).
Identification of the amino acid residue in the nematode galectin LEC-1 responsible for its unique sugar binding property: analysis by combination of site-directed mutagenesis and frontal affinity chromatography.
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Biol Pharm Bull,
30,
2012-2017.
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T.Shirai,
C.Shionyu-Mitsuyama,
T.Ogawa,
and
K.Muramoto
(2006).
Structure based studies of the adaptive diversification process of congerins.
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Mol Divers,
10,
567-573.
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C.Seelenmeyer,
S.Wegehingel,
I.Tews,
M.Künzler,
M.Aebi,
and
W.Nickel
(2005).
Cell surface counter receptors are essential components of the unconventional export machinery of galectin-1.
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J Cell Biol,
171,
373-381.
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M.Ambrosi,
N.R.Cameron,
and
B.G.Davis
(2005).
Lectins: tools for the molecular understanding of the glycocode.
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Org Biomol Chem,
3,
1593-1608.
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G.R.Vasta,
H.Ahmed,
and
E.W.Odom
(2004).
Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates.
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Curr Opin Struct Biol,
14,
617-630.
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M.S.Sujatha,
and
P.V.Balaji
(2004).
Identification of common structural features of binding sites in galactose-specific proteins.
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Proteins,
55,
44-65.
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N.G.Than,
E.Pick,
S.Bellyei,
A.Szigeti,
O.Burger,
Z.Berente,
T.Janaky,
A.Boronkai,
H.Kliman,
H.Meiri,
H.Bohn,
G.N.Than,
and
B.Sumegi
(2004).
Functional analyses of placental protein 13/galectin-13.
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Eur J Biochem,
271,
1065-1078.
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J.D.Schrag,
D.O.Procopio,
M.Cygler,
D.Y.Thomas,
and
J.J.Bergeron
(2003).
Lectin control of protein folding and sorting in the secretory pathway.
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Trends Biochem Sci,
28,
49-57.
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M.G.Ford,
T.Weimar,
T.Köhli,
and
R.J.Woods
(2003).
Molecular dynamics simulations of galectin-1-oligosaccharide complexes reveal the molecular basis for ligand diversity.
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Proteins,
53,
229-240.
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M.La,
T.V.Cao,
G.Cerchiaro,
K.Chilton,
J.Hirabayashi,
K.Kasai,
S.M.Oliani,
Y.Chernajovsky,
and
M.Perretti
(2003).
A novel biological activity for galectin-1: inhibition of leukocyte-endothelial cell interactions in experimental inflammation.
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Am J Pathol,
163,
1505-1515.
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K.Scott,
and
J.Zhang
(2002).
Partial identification by site-directed mutagenesis of a cell growth inhibitory site on the human galectin-1 molecule.
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BMC Cell Biol,
3,
3.
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J.W.Dennis,
C.E.Warren,
M.Granovsky,
and
M.Demetriou
(2001).
Genetic defects in N-glycosylation and cellular diversity in mammals.
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Curr Opin Struct Biol,
11,
601-607.
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H.Zhang,
K.Huang,
Z.Li,
L.Banerjei,
K.E.Fisher,
N.V.Grishin,
E.Eisenstein,
and
O.Herzberg
(2000).
Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 A resolution: functional implications.
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Proteins,
40,
86-97.
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PDB codes:
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M.A.Bianchet,
H.Ahmed,
G.R.Vasta,
and
L.M.Amzel
(2000).
Soluble beta-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes.
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Proteins,
40,
378-388.
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PDB codes:
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M.Sahin-Tóth,
K.M.Akhoon,
J.Runner,
and
H.R.Kaback
(2000).
Ligand recognition by the lactose permease of Escherichia coli: specificity and affinity are defined by distinct structural elements of galactopyranosides.
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Biochemistry,
39,
5097-5103.
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R.Ramkumar,
and
S.K.Podder
(2000).
Elucidation of the mechanism of interaction of sheep spleen galectin-1 with splenocytes and its role in cell-matrix adhesion.
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J Mol Recognit,
13,
299-309.
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J.Bouckaert,
T.Hamelryck,
L.Wyns,
and
R.Loris
(1999).
Novel structures of plant lectins and their complexes with carbohydrates.
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Curr Opin Struct Biol,
9,
572-577.
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J.M.Rini,
and
Y.D.Lobsanov
(1999).
New animal lectin structures.
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Curr Opin Struct Biol,
9,
578-584.
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M.M.Prabu,
K.Suguna,
and
M.Vijayan
(1999).
Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins.
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Proteins,
35,
58-69.
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T.Ogawa,
C.Ishii,
D.Kagawa,
K.Muramoto,
and
H.Kamiya
(1999).
Accelerated evolution in the protein-coding region of galectin cDNAs, congerin I and congerin II, from skin mucus of conger eel (Conger myriaster).
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Biosci Biotechnol Biochem,
63,
1203-1208.
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T.Shirai,
C.Mitsuyama,
Y.Niwa,
Y.Matsui,
H.Hotta,
T.Yamane,
H.Kamiya,
C.Ishii,
T.Ogawa,
and
K.Muramoto
(1999).
High-resolution structure of the conger eel galectin, congerin I, in lactose-liganded and ligand-free forms: emergence of a new structure class by accelerated evolution.
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Structure,
7,
1223-1233.
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PDB codes:
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D.D.Leonidas,
E.H.Vatzaki,
H.Vorum,
J.E.Celis,
P.Madsen,
and
K.R.Acharya
(1998).
Structural basis for the recognition of carbohydrates by human galectin-7.
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Biochemistry,
37,
13930-13940.
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PDB codes:
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O.Kobayashi,
N.Hayashi,
R.Kuroki,
and
H.Sone
(1998).
Region of FLO1 proteins responsible for sugar recognition.
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J Bacteriol,
180,
6503-6510.
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R.Y.Yang,
P.N.Hill,
D.K.Hsu,
and
F.T.Liu
(1998).
Role of the carboxyl-terminal lectin domain in self-association of galectin-3.
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Biochemistry,
37,
4086-4092.
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C.S.Wright
(1997).
New folds of plant lectins.
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Curr Opin Struct Biol,
7,
631-636.
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H.C.Siebert,
R.Adar,
R.Arango,
M.Burchert,
H.Kaltner,
G.Kayser,
E.Tajkhorshid,
C.W.von der Lieth,
R.Kaptein,
N.Sharon,
J.F.Vliegenthart,
and
H.J.Gabius
(1997).
Involvement of laser photo-CIDNP (chemically induced dynamic nuclear polarization)-reactive amino acid side chains in ligand binding by galactoside-specific lectins in solution.
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Eur J Biochem,
249,
27-38.
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H.J.Gabius
(1997).
Animal lectins.
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Eur J Biochem,
243,
543-576.
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T.R.Transue,
A.K.Smith,
H.Mo,
I.J.Goldstein,
and
M.A.Saper
(1997).
Structure of benzyl T-antigen disaccharide bound to Amaranthus caudatus agglutinin.
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Nat Struct Biol,
4,
779-783.
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PDB codes:
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C.S.Wright,
and
G.Hester
(1996).
The 2.0 A structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: evidence for two unique binding modes.
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Structure,
4,
1339-1352.
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PDB code:
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J.I.Lee,
M.F.Varela,
and
T.H.Wilson
(1996).
Physiological evidence for an interaction between Glu-325 and His-322 in the lactose carrier of Escherichia coli.
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Biochim Biophys Acta,
1278,
111-118.
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M.Cho,
and
R.D.Cummings
(1996).
Characterization of monomeric forms of galectin-1 generated by site-directed mutagenesis.
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Biochemistry,
35,
13081-13088.
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M.T.Elola,
and
N.E.Fink
(1996).
Purification and partial biochemical characterization of an S-type lectin from blastula embryos of Bufo arenarum.
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Comp Biochem Physiol B Biochem Mol Biol,
115,
175-182.
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R.Y.Yang,
D.K.Hsu,
and
F.T.Liu
(1996).
Expression of galectin-3 modulates T-cell growth and apoptosis.
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Proc Natl Acad Sci U S A,
93,
6737-6742.
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S.Rosén,
M.Kata,
Y.Persson,
P.H.Lipniunas,
M.Wikström,
M.J.Van Den Hondel,
J.Van Den Brink,
L.Rask,
L.O.Hedén,
and
A.Tunlid
(1996).
Molecular characterization of a saline-soluble lectin from a parasitic fungus. Extensive sequence similarities between fungal lectins.
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Eur J Biochem,
238,
822-829.
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D.D.Leonidas,
B.L.Elbert,
Z.Zhou,
H.Leffler,
S.J.Ackerman,
and
K.R.Acharya
(1995).
Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins.
|
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Structure,
3,
1379-1393.
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PDB code:
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D.Fowlis,
C.Colnot,
M.A.Ripoche,
and
F.Poirier
(1995).
Galectin-3 is expressed in the notochord, developing bones, and skin of the postimplantation mouse embryo.
|
| |
Dev Dyn,
203,
241-251.
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D.I.Stuart,
and
E.Y.Jones
(1995).
Recognition at the cell surface: recent structural insights.
|
| |
Curr Opin Struct Biol,
5,
735-743.
|
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E.K.Schweda,
J.A.Jonasson,
and
P.E.Jansson
(1995).
Structural studies of lipooligosaccharides from Haemophilus ducreyi ITM 5535, ITM 3147, and a fresh clinical isolate, ACY1: evidence for intrastrain heterogeneity with the production of mutually exclusive sialylated or elongated glycoforms.
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J Bacteriol,
177,
5316-5321.
|
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J.M.Rini
(1995).
X-ray crystal structures of animal lectins.
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| |
Curr Opin Struct Biol,
5,
617-621.
|
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K.Drickamer
(1995).
Multiplicity of lectin-carbohydrate interactions.
|
| |
Nat Struct Biol,
2,
437-439.
|
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K.Drickamer
(1995).
Increasing diversity of animal lectin structures.
|
| |
Curr Opin Struct Biol,
5,
612-616.
|
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M.Fukuda
(1995).
Carbohydrate-dependent cell adhesion.
|
| |
Bioorg Med Chem,
3,
207-215.
|
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M.Menéndez,
M.Gasset,
J.Laynez,
C.López-Zumel,
P.Usobiaga,
E.Töpfer-Petersen,
and
J.J.Calvete
(1995).
Analysis of the structural organization and thermal stability of two spermadhesins. Calorimetric, circular dichroic and Fourier-transform infrared spectroscopic studies.
|
| |
Eur J Biochem,
234,
887-896.
|
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S.B.Engelsen,
J.Koca,
I.Braccini,
C.Hervé du Penhoat,
and
S.Pérez
(1995).
Travelling on the potential energy surfaces of carbohydrates: comparative application of an exhaustive systematic conformational search with an heuristic search.
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| |
Carbohydr Res,
276,
1.
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S.Schröder,
F.Schimmöller,
B.Singer-Krüger,
and
H.Riezman
(1995).
The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the ret1-1 mutation in alpha-COP.
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| |
J Cell Biol,
131,
895-912.
|
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D.Solís,
J.Jiménez-Barbero,
M.Martín-Lomas,
and
T.Díaz-Mauriño
(1994).
Probing hydrogen-bonding interactions of bovine heart galectin-1 and methyl beta-lactoside by use of engineered ligands.
|
| |
Eur J Biochem,
223,
107-114.
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J.Hirabayashi,
and
K.Kasai
(1994).
Further evidence by site-directed mutagenesis that conserved hydrophilic residues form a carbohydrate-binding site of human galectin-1.
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Glycoconj J,
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N.Sharon
(1994).
When lectin meets oligosaccharide.
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Nat Struct Biol,
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N.Srinivasan,
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(1994).
Comparative analyses of pentraxins: implications for protomer assembly and ligand binding.
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Structure,
2,
1017-1027.
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PDB codes:
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S.H.Barondes,
V.Castronovo,
D.N.Cooper,
R.D.Cummings,
K.Drickamer,
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C.Hughes,
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Galectins: a family of animal beta-galactoside-binding lectins.
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Cell,
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Y.Bourne,
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Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides.
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863-870.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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