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PDBsum entry 1lob
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Contents |
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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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Three-Dimensional structures of complexes of lathyrus ochrus isolectin i with glucose and mannose: fine specificity of the monosaccharide-Binding site.
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Authors
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Y.Bourne,
A.Roussel,
M.Frey,
P.Rougé,
J.C.Fontecilla-Camps,
C.Cambillau.
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Ref.
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Proteins, 1990,
8,
365-376.
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PubMed id
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Abstract
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The structure of the methyl-alpha-D-mannopyranoside-LOL I complex has been
solved by the molecular replacement method using the refined saccharide-free LOL
I coordinates as starting model. The methyl-alpha-D-mannopyranoside-LOL I
complex was refined by simulated annealing using the program X-PLOR. The final
R-factor value is 0.182 [Fo greater than 1 sigma(Fo)]. The isostructural
methyl-alpha-D-glucopyranoside-LOL I complex was refined by X-Ray coupled energy
minimization using the methyl-alpha-D-mannopyranoside-LOL I structure as a
starting model to an R factor of 0.179 (all data). In both crystal forms, each
dimer binds two molecules of sugar in pockets found near the calcium ions. The
two saccharide moieties, which are in the C1 chair conformation, establish the
same hydrogen bond pattern with the lectin. However, the van der Waals contacts
are different between the O2, C2, C6, and O6 atoms of the two molecules and the
backbone atoms of residues 208-211. Mannose, due to its axial C2 conformation,
encloses the backbone atoms of the protein in a clamplike way. Van der Waals
energy calculations suggest that this better complementarity of the mannoside
molecule with the lectin could explain its higher affinity for isolectin I.
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray studies of two isolectins from the seeds of lathyrus ochrus.
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Authors
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Y.Bourne,
P.Rougé,
C.Cambillau.
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Ref.
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J Mol Biol, 1988,
202,
685-687.
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PubMed id
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