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PDBsum entry 4xbl
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Sugar binding protein
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PDB id
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4xbl
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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 underlying the binding preference of human galectins-1, -3 and -7 for galβ1-3/4glcnac.
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Authors
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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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Ref.
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Plos One, 2015,
10,
e0125946.
[DOI no: ]
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PubMed id
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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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