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PDBsum entry 4xbn
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Sugar binding protein
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PDB id
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4xbn
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PDB id:
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| Name: |
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Sugar binding protein
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Title:
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Crystal structure of human galectin-3 crd in complex with type 1 n- acetyllactosamine
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Structure:
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Galectin-3. Chain: a. Fragment: carbohydrate recognition domain (unp residues 113-250). Synonym: gal-3,35 kda lectin,carbohydrate-binding protein 35,cbp 35, galactose-specific lectin 3,galactoside-binding protein,galbp,ige- binding protein,l-31,laminin-binding protein,lectin l-29,mac-2 antigen. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: lgals3, mac2. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.21Å
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R-factor:
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0.168
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R-free:
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0.203
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Authors:
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T.J.Hsieh,H.Y.Lin,C.H.Lin
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Key ref:
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T.J.Hsieh
et al.
(2015).
Structural Basis Underlying the Binding Preference of Human Galectins-1, -3 and -7 for Galβ1-3/4GlcNAc.
Plos One,
10,
e0125946.
PubMed id:
DOI:
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Date:
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17-Dec-14
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Release date:
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20-May-15
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PROCHECK
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Headers
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References
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P17931
(LEG3_HUMAN) -
Galectin-3 from Homo sapiens
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Seq:
Struc:
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250 a.a.
138 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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DOI no:
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Plos One
10:e0125946
(2015)
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PubMed id:
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Structural Basis Underlying the Binding Preference of Human Galectins-1, -3 and -7 for Galβ1-3/4GlcNAc.
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T.J.Hsieh,
H.Y.Lin,
Z.Tu,
B.S.Huang,
S.C.Wu,
C.H.Lin.
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ABSTRACT
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Galectins represent β-galactoside-binding proteins and are known to bind
Galβ1-3/4GlcNAc disaccharides (abbreviated as LN1 and LN2, respectively).
Despite high sequence and structural homology shared by the carbohydrate
recognition domain (CRD) of all galectin members, how each galectin displays
different sugar-binding specificity still remains ambiguous. Herein we provided
the first structural evidence of human galectins-1, 3-CRD and 7 in complex with
LN1. Galectins-1 and 3 were shown to have higher affinity for LN2 than for LN1,
while galectin-7 displayed the reversed specificity. In comparison with the
previous LN2-complexed structures, the results indicated that the average
glycosidic torsion angle of galectin-bound LN1 (ψLN1 ≈ 135°) was
significantly differed from that of galectin-bound LN2 (ψLN2 ≈ -108°), i.e.
the GlcNAc moiety adopted a different orientation to maintain essential
interactions. Furthermore, we also identified an Arg-Asp/Glu-Glu-Arg salt-bridge
network and the corresponding loop (to position the second Asp/Glu residue)
critical for the LN1/2-binding preference.
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