6hku | pdb_00006hku

Trichodysplasia spinulosa-associated polyomavirus (TSPyV) VP1 in complex with sialylated precision glycooligomers

spinqualitylabelsall models 6hku, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6hku is a 10 chain structure with sequence from Tspyv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GAL, GLC, GOL, SIA Gene: VP1 (TSPyV) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Divalent precision glycooligomers terminating in N-acetylneuraminic acid (Neu5Ac) or 3'-sialyllactose (3'-SL) with varying linkers between scaffold and the glycan portions are synthesized via solid phase synthesis for co-crystallization studies with the sialic acid-binding major capsid protein VP1 of human Trichodysplasia spinulosa-associated Polyomavirus. High-resolution crystal structures of complexes demonstrate that the compounds bind to VP1 depending on the favorable combination of carbohydrate ligand and linker. It is found that artificial linkers can replace portions of natural carbohydrate linkers as long as they meet certain requirements such as size or flexibility to optimize contact area between ligand and receptor binding sites. The obtained results will influence the design of future high affinity ligands based on the structures presented here, and they can serve as a blueprint to develop multivalent glycooligomers as inhibitors of viral adhesion. Divalent Sialylated Precision Glycooligomers Binding to Polyomaviruses and the Effect of Different Linkers.,Baier M, Rustmeier NH, Harr J, Cyrus N, Reiss GJ, Grafmuller A, Blaum BS, Stehle T, Hartmann L Macromol Biosci. 2019 Mar 18:e1800426. doi: 10.1002/mabi.201800426. PMID:30884172 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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