2KR2
Xenopus laevis malectin complexed with maltose (Glcalpha1-4Glc)
Summary for 2KR2
| Entry DOI | 10.2210/pdb2kr2/pdb |
| Related | 2JWP 2K46 |
| Related PRD ID | PRD_900018 |
| Descriptor | Malectin-A, alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | lectin/carbohydrate, carbohydrate metabolism, endoplasmic reticulum, glycoprotein, membrane, transmembrane, carbohydrate binding protein |
| Biological source | Xenopus laevis (clawed frog,common platanna,platanna) |
| Cellular location | Endoplasmic reticulum membrane; Single-pass type I membrane protein: Q6INX3 |
| Total number of polymer chains | 1 |
| Total formula weight | 21542.30 |
| Authors | Schallus, T.,Feher, K.,Muhle-Goll, C. (deposition date: 2009-11-30, release date: 2010-07-14, Last modification date: 2024-05-01) |
| Primary citation | Schallus, T.,Feher, K.,Sternberg, U.,Rybin, V.,Muhle-Goll, C. Analysis of the specific interactions between the lectin domain of malectin and diglucosides. Glycobiology, 20:1010-1020, 2010 Cited by PubMed 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. PubMed: 20466650DOI: 10.1093/glycob/cwq059 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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