9CMO

Cryo-EM model derived from localized reconstruction of Ad657-hexon-FII complex at 4.14A resolution

9CMO の概要

• エントリーDOI: 10.2210/pdb9cmo/pdb
• 関連するPDBエントリー: 9CM2 9CM9
• EMDBエントリー: 45751
• 分子名称: Hexon protein, Prothrombin, CALCIUM ION (3 entities in total)
• 機能のキーワード: adenovirus, hexon, coagulation factor x, coagulation factor ii, prothrombin, complex, interactions, virus, viral protein
• 由来する生物種: Human adenovirus 6; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 395615.69

構造登録者

Reddy, V.S.,Ma, O.X. (登録日: 2024-07-15, 公開日: 2024-11-27)

主引用文献

Mudrick, H.E.,Lu, S.C.,Bhandari, J.,Barry, M.E.,Hemsath, J.R.,Andres, F.G.M.,Ma, O.X.,Barry, M.A.,Reddy, V.S.
Structure-derived insights from blood factors binding to the surfaces of different adenoviruses.
Nat Commun, 15:9768-9768, 2024

PubMed Abstract: The tropism of adenoviruses (Ads) is significantly influenced by the binding of various blood factors. To investigate differences in their binding, we conducted cryo-EM analysis on complexes of several human adenoviruses with human platelet factor-4 (PF4), coagulation factors FII (Prothrombin), and FX. While we observed EM densities for FII and FX bound to all the species-C adenoviruses examined, no densities were seen for PF4, even though PF4 can co-pellet with various Ads. Similar to FX, the γ-carboxyglutamic acid (Gla) domain of FII binds within the surface cavity of hexon trimers. While FII binds equally to species-C Ads: Ad5, Ad6, and Ad657, FX exhibits significantly better binding to Ad5 and Ad657 compared to Ad6. Although only the FX-Gla domain is observed at high-resolution (3.7 Å), the entire FX is visible at low-resolution bound to Ad5 in three equivalent binding modes consistent with the 3-fold symmetric hexon. Only the Gla and kringle-1 domains of FII are visible on all the species-C adenoviruses, where the rigid FII binds in an upright fashion, in contrast to the flexible and bent FX. These data suggest that differential binding of FII and FX may shield certain species-C adenoviruses differently against immune molecules, thereby modulating their tropism.

PubMed: 39528527
DOI: 10.1038/s41467-024-54049-9

実験手法

ELECTRON MICROSCOPY (4.17 Å)