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Analysis of the specific interactions between the lectin domain of malectin and diglucosides
- Source :
- Glycobiology. 20:1010-1020
- Publication Year :
- 2010
- Publisher :
- Oxford University Press (OUP), 2010.
-
Abstract
- The endoplasmic reticulum malectin is a highly conserved protein in the animal kingdom that has no counterpart so far in lower organisms. We recently determined the structure of its conserved domain and found a highly selective binding to Glc(2)Man(9)GlcNAc(2), an intermediate of N-glycosylation. In our quest for putative ligands during the initial characterization of the protein, we noticed that the malectin domain is highly specific for diglucosides but quite tolerant towards the linkage of the glucosidic bond. To understand the molecular requirements for the observed promiscuity of the malectin domain, here we analyze the binding to a range of diglucosides through comparison of the protein chemical shift perturbation patterns and the saturation transfer difference spectra of the ligands including two maltose-mimicking drugs. A comparison of the maltose-bound structure of the malectin domain with the complex of the native ligand nigerose reveals why malectin is able to tolerate such a diversity of ligands.
- Subjects :
- Models, Molecular
Magnetic Resonance Spectroscopy
Ligand
Endoplasmic reticulum
Protein domain
Nigerose
Carbohydrate-binding protein
Membrane Proteins
Lectin
Reference Standards
Biology
Endoplasmic Reticulum
Highly selective
Biochemistry
Protein Structure, Tertiary
Xenopus laevis
chemistry.chemical_compound
Glucosides
chemistry
Saturation transfer
Lectins
biology.protein
Animals
Subjects
Details
- ISSN :
- 14602423 and 09596658
- Volume :
- 20
- Database :
- OpenAIRE
- Journal :
- Glycobiology
- Accession number :
- edsair.doi.dedup.....f502a59320f2798ed040e79336286ebd
- Full Text :
- https://doi.org/10.1093/glycob/cwq059