1w6p
X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1 COMPLEXED WITH N-ACETYL-LACTOSAMINE
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OverviewOverview
Human galectin-1 is a potent multifunctional effector that participates in, specific protein-carbohydrate and protein-protein (lipid) interactions. By, determining its X-ray structure, we provide the basis to define the, structure of its ligand-binding pocket and to perform rational drug, design. We have also analysed whether single-site mutations introduced at, some distance from the carbohydrate recognition domain can affect the, lectin fold and influence sugar binding. Both the substitutions introduced, in the C2S and R111H mutants altered the presentation of the loop, harbouring Asp123 in the common "jelly-roll" fold. The orientation of the, side-chain was inverted 180 degrees and the positions of two key residues, in the sugar-binding site of the R111H mutant were notably shifted, ... [(full description)]
About this StructureAbout this Structure
1W6P is a [Single protein] structure of sequence from [Homo sapiens] with SO4 and BME as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding., Lopez-Lucendo MF, Solis D, Andre S, Hirabayashi J, Kasai K, Kaltner H, Gabius HJ, Romero A, J Mol Biol. 2004 Oct 29;343(4):957-70. PMID:15476813
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