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PDBsum entry 2eal
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Sugar binding protein
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PDB id
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2eal
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Contents |
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* Residue conservation analysis
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PDB id:
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Sugar binding protein
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Title:
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Crystal structure of human galectin-9 n-terminal crd in complex with forssman pentasaccharide
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Structure:
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Galectin-9. Chain: a, b. Fragment: n-terminal domain. Synonym: hom-hd-21, ecalectin. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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1.85Å
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R-factor:
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0.209
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R-free:
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0.245
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Authors:
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M.Nagae,S.Nakamura-Tsuruta,N.Nishi,T.Nakamura,J.Hirabayashi, S.Wakatsuki,R.Kato
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Key ref:
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M.Nagae
et al.
(2008).
Structural analysis of the human galectin-9 N-terminal carbohydrate recognition domain reveals unexpected properties that differ from the mouse orthologue.
J Mol Biol,
375,
119-135.
PubMed id:
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Date:
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31-Jan-07
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Release date:
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25-Sep-07
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PROCHECK
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Headers
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References
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O00182
(LEG9_HUMAN) -
Galectin-9 from Homo sapiens
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Seq:
Struc:
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355 a.a.
141 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 Mol Biol
375:119-135
(2008)
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PubMed id:
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Structural analysis of the human galectin-9 N-terminal carbohydrate recognition domain reveals unexpected properties that differ from the mouse orthologue.
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M.Nagae,
N.Nishi,
S.Nakamura-Tsuruta,
J.Hirabayashi,
S.Wakatsuki,
R.Kato.
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ABSTRACT
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Galectins are a family of beta-galactoside-binding lectins that contain a
conserved carbohydrate recognition domain (CRD). They exhibit high affinities
for small beta-galactosides as well as variable binding specificities for
complex glycoconjugates. Structural and biochemical analyses of the mechanism
governing specific carbohydrate recognition provide a useful template to
elucidate the function of these proteins. Here we report the crystal structures
of the human galectin-9 N-terminal CRD (NCRD) in the presence of lactose and
Forssman pentasaccharide. Mouse galectin-9 NCRD, the structure of which was
previously solved by our group, forms a non-canonical dimer in both the crystal
state and in solution. Human galectin-9 NCRD, however, exists as a monomer in
crystals, despite a high sequence identity to the mouse homologue. Comparative
frontal affinity chromatography analysis of the mouse and human galectin-9 NCRDs
revealed different carbohydrate binding specificities, with disparate affinities
for complex glycoconjugates. Human galectin-9 NCRD exhibited a high affinity for
Forssman pentasaccharide; the association constant for mouse galectin-9 NCRD was
100-fold less than that observed for the human protein. The combination of
structural data with mutational studies demonstrated that non-conserved amino
acid residues on the concave surface were important for determination of target
specificities. The human galectin-9 NCRD exhibited greater inhibition of cell
proliferation than the mouse NCRD. We discuss the biochemical and structural
differences between highly homologous proteins from different species.
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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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S.Bi,
L.A.Earl,
L.Jacobs,
and
L.G.Baum
(2008).
Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways.
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J Biol Chem,
283,
12248-12258.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
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.
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Links
