6HKV

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

6HKV の概要

• エントリーDOI: 10.2210/pdb6hkv/pdb
• 分子名称: Capsid protein VP1, Sialylated precision glycomacromolecule, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: sialic acid derivative, viral protein
• 由来する生物種: Trichodysplasia spinulosa-associated polyomavirus
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 323737.90

構造登録者

Rustmeier, N.H.,Stehle, T. (登録日: 2018-09-08, 公開日: 2019-03-27, 最終更新日: 2024-01-17)

主引用文献

Baier, M.,Rustmeier, N.H.,Harr, J.,Cyrus, N.,Reiss, G.J.,Grafmuller, A.,Blaum, B.S.,Stehle, T.,Hartmann, L.
Divalent Sialylated Precision Glycooligomers Binding to Polyomaviruses and the Effect of Different Linkers.
Macromol Biosci, 19:e1800426-e1800426, 2019

PubMed Abstract: 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.

PubMed: 30884172
DOI: 10.1002/mabi.201800426

実験手法

X-RAY DIFFRACTION (1.75 Å)