CRYSTAL-STRUCTURE OF HUMAN RHINOVIRUS SEROTYPE-1A (HRV1A)
CRYSTAL-STRUCTURE OF HUMAN RHINOVIRUS SEROTYPE-1A (HRV1A)
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DOI：
10.1016/0022-2836(89)90293-3
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发表时间：
1989-11-05
影响因子：
5.6
通讯作者：
MCKINLAY, MA
中科院分区：
文献类型：
--
作者：
KIM, S;SMITH, TJ;MCKINLAY, MA
人鼻病毒1A （HRV1A）的结构已测定为3.2 . ang。采用相位细化和扩展的对称平均，从相位在5 . ang开始。根据已知的人鼻病毒14 （HRV14）结构计算的分辨率。HRV1A和HRV14的多肽主链结构相似，但暴露表面有较大差异。在假定的受体结合位点“峡谷”中，氨基酸残基的不同电荷分布可能解释了以HRV1A和HRV14分别为代表的次要和主要受体组特异性的差异。VP1中抗病毒化合物结合的疏水袋呈“开放”构象，类似于在药物结合的HRV14中观察到的。与HRV14不同，HRV1A的药物结合不会引起广泛的构象变化。
The structure of human rhinovirus 1A (HRV1A) has been determined to 3.2 .ANG. resolution using phase refinement and extension by symmetry averaging starting with phases at 5 .ANG. resolution calculated from the known human rhinovirus 14 (HRV14) structure. The polypeptide backbone structures of HRV1A and HRV14 are similar, but the exposed surfaces are rather different. Differential charge distribution of amino acid residues in the "canyon", the putative receptor binding site, provides a possible explanation for the difference in minor versus major receptor group specificities, represented by HRV1A and HRV14, respectively. The hydrophobic pocket in VP1, into which antiviral compounds bind, is in an "open" conformation similar to that observed in drug-bound HRV14. Drug binding in HRV1A does not induce extensive conformational changes, in contrast to the case of HRV14.