首页> 美国卫生研究院文献>Neurology International >Amino Acid Sequences Mediating Vascular Cell Adhesion Molecule 1 Binding to Integrin Alpha 4: Homologous DSP Sequence Found for JC Polyoma VP1 Coat Protein
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Amino Acid Sequences Mediating Vascular Cell Adhesion Molecule 1 Binding to Integrin Alpha 4: Homologous DSP Sequence Found for JC Polyoma VP1 Coat Protein

机译:介导血管细胞粘附分子1结合整合素α4的氨基酸序列:发现JC多瘤VP1外壳蛋白的同源DSP序列。

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摘要

The JC polyoma viral coat protein VP1 was analyzed for amino acid sequences homologies to the IDSP sequence which mediates binding of VLA-4 (integrin alpha 4) to vascular cell adhesion molecule 1. Although the full sequence was not found, a DSP sequence was located near the critical arginine residue linked to infectivity of the virus and binding to sialic acid containing molecules such as integrins (3). For the JC polyoma virus, a DSP sequence was found at residues 70, 71 and 72 with homology also noted for the mouse polyoma virus and SV40 virus. Three dimensional modeling of the VP1 molecule suggests that the DSP loop has an accessible site for interaction from the external side of the assembled viral capsid pentamer.
机译:分析了JC多瘤病毒外壳蛋白VP1的氨基酸序列与IDSP序列的同源性,该IDSP序列介导VLA-4(整合素α4)与血管细胞粘附分子1的结合。尽管未找到完整序列,但找到了DSP序列关键的精氨酸残基附近与病毒的感染性相关并与包含唾液酸的分子(如整联蛋白)结合(3)。对于JC多瘤病毒,在残基70、71和72处发现了DSP序列,并且与小鼠多瘤病毒和SV40病毒也具有同源性。 VP1分子的三维建模表明,DSP环具有可访问的位置,可从组装的病毒衣壳五聚体的外侧进行相互作用。

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