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Title
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Crystal structure of the complex of concanavalin A and tripeptide.
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Authors
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Z.Zhang,
M.Qian,
Q.Huang,
Y.Jia,
Y.Tang,
K.Wang,
D.Cui,
M.Li.
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Ref.
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J Protein Chem, 2001,
20,
59-65.
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PubMed id
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Abstract
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The X-ray structure analysis of a cross-linked crystal of concanavalin A soaked
with the tripeptide molecule as the probe molecule showed electron density
corresponding to full occupation in the binding pocket. The site lies on the
surface of concanavalin A and is surrounded by three symmetry-related molecules.
The crystal structure of the tripeptide complex was refined at 2.4-A resolution
to an R-factor of 17.5%, (Rfree factor of 23.7%), with an RMS deviation in bond
distances of 0.01 A. The model includes all 237 residue of concanavalin A, 1
manganese ion, 1 calcium ion, 161 water molecules, 1 glutaraldehyde molecule,
and 1 tripeptide molecule. This X-ray structure analysis also provides an
approach to mapping the binding surface of crystalline protein with a probe
molecule that is dissolved in a mixture of organic solvent with water or in neat
organic solvent but is hardly dissolved in aqueous solution.
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