Verdaguer Nuria, Fita Ignacio, Reithmayer Manuela, Moser Rosita, Blaas Dieter
Institut de Biologia Molecular de Barcelona, Consejo Superior de Investigaciones Científicas, Jordi Girona 18-26, E-08034 Barcelona, Spain.
Nat Struct Mol Biol. 2004 May;11(5):429-34. doi: 10.1038/nsmb753. Epub 2004 Apr 4.
Although many viral receptors have been identified, the ways in which they interact with their cognate viruses are not understood at the molecular level. We have determined the X-ray structure of a complex between calcium-containing modules of the very low-density lipoprotein receptor and the minor group human rhinovirus HRV2. The receptor binds close to the icosahedral five-fold vertex, with only one module per virus protomer. The binding face of this module is defined by acidic calcium-chelating residues and, in particular, by an exposed tryptophan that is highly conserved. The attachment site on the virus involves only residues from VP1, particularly a lysine strictly conserved in all minor group HRVs. The disposition of the attached ligand-binding repeats around the five-fold axis, together with the proximity of the N- and C-terminal ends of adjacent modules, suggests that more than one repeat in a single receptor molecule might attach simultaneously.
尽管已鉴定出许多病毒受体，但它们在分子水平上与同源病毒相互作用的方式仍不清楚。我们确定了极低密度脂蛋白受体含钙模块与B组人鼻病毒HRV2之间复合物的X射线结构。受体结合在二十面体五重轴附近，每个病毒原体仅有一个模块。该模块的结合面由酸性钙螯合残基界定，特别是由一个高度保守的暴露色氨酸界定。病毒上的附着位点仅涉及VP1的残基，特别是在所有B组鼻病毒中严格保守的一个赖氨酸。附着的配体结合重复序列围绕五重轴的排列，以及相邻模块N端和C端的接近程度，表明单个受体分子中的多个重复序列可能同时附着。
