Querol-Audí Jordi, Konecsni Tuende, Pous Joan, Carugo Oliviero, Fita Ignasi, Verdaguer Nuria, Blaas Dieter
Institut de Biologia Molecular de Barcelona (CSIC), Parc Científic de Barcelona, Barcelona, Spain.
FEBS Lett. 2009 Jan 5;583(1):235-40. doi: 10.1016/j.febslet.2008.12.014. Epub 2008 Dec 13.
X-ray structures of human rhinovirus 2 (HRV2) in complex with soluble very-low-density lipoprotein receptors encompassing modules 1, 2, and 3 (V123) and five V3 modules arranged in tandem (V33333) demonstrates multi-modular binding around the virion's five-fold axes. Occupancy was 60% for V123 and 100% for V33333 explaining the high-avidity of the interaction. Surface potentials of 3D-models of all minor group HRVs and K-type major group HRVs were compared; hydrophobic interactions between a conserved lysine in the viruses and a tryptophan in the receptor modules together with coulombic attraction via diffuse opposite surface potentials determine minor group HRV receptor specificity.
人鼻病毒2型（HRV2）与包含模块1、2和3的可溶性极低密度脂蛋白受体（V123）以及串联排列的五个V3模块（V33333）形成复合物的X射线结构显示，在病毒粒子的五重轴周围存在多模块结合。V123的占有率为60%，V33333的占有率为100%，这解释了相互作用的高亲和力。比较了所有B亚组HRV和K型A亚组HRV的三维模型的表面电位；病毒中保守赖氨酸与受体模块中色氨酸之间的疏水相互作用，以及通过弥散的相反表面电位产生的库仑吸引力决定了B亚组HRV受体的特异性。
