3PUN
Crystal structure of P domain dimer of Norovirus VA207 with Lewis y tetrasaccharide
3PUN の概要
| エントリーDOI | 10.2210/pdb3pun/pdb |
| 関連するPDBエントリー | 3PUM 3PVD |
| 関連するBIRD辞書のPRD_ID | PRD_900124 |
| 分子名称 | Capsid, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-alpha-D-glucopyranose (3 entities in total) |
| 機能のキーワード | greek key, mixed alpha/beta structure, receptor binding, carbohydrate/sugar binding, capsid, viral protein |
| 由来する生物種 | Human calicivirus |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 70700.56 |
| 構造登録者 | |
| 主引用文献 | Chen, Y.,Tan, M.,Xia, M.,Hao, N.,Zhang, X.C.,Huang, P.,Jiang, X.,Li, X.,Rao, Z. Crystallography of a Lewis-binding norovirus, elucidation of strain-specificity to the polymorphic human histo-blood group antigens Plos Pathog., 7:e1002152-e1002152, 2011 Cited by PubMed Abstract: Noroviruses, an important cause of acute gastroenteritis in humans, recognize the histo-blood group antigens (HBGAs) as host susceptible factors in a strain-specific manner. The crystal structures of the HBGA-binding interfaces of two A/B/H-binding noroviruses, the prototype Norwalk virus (GI.1) and a predominant GII.4 strain (VA387), have been elucidated. In this study we determined the crystal structures of the P domain protein of the first Lewis-binding norovirus (VA207, GII.9) that has a distinct binding property from those of Norwalk virus and VA387. Co-crystallization of the VA207 P dimer with Le(y) or sialyl Le(x) tetrasaccharides showed that VA207 interacts with these antigens through a common site found on the VA387 P protein which is highly conserved among most GII noroviruses. However, the HBGA-binding site of VA207 targeted at the Lewis antigens through the α-1, 3 fucose (the Lewis epitope) as major and the β-N-acetyl glucosamine of the precursor as minor interacting sites. This completely differs from the binding mode of VA387 and Norwalk virus that target at the secretor epitopes. Binding pocket of VA207 is formed by seven amino acids, of which five residues build up the core structure that is essential for the basic binding function, while the other two are involved in strain-specificity. Our results elucidate for the first time the genetic and structural basis of strain-specificity by a direct comparison of two genetically related noroviruses in their interaction with different HBGAs. The results provide insight into the complex interaction between the diverse noroviruses and the polymorphic HBGAs and highlight the role of human HBGA as a critical factor in norovirus evolution. PubMed: 21811409DOI: 10.1371/journal.ppat.1002152 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.05 Å) |
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