细胞间粘附分子-1（ICAM-1）的结构域结构及与鼻病毒结合的动力学
The domain structure of ICAM-1 and the kinetics of binding to rhinovirus.
作者信息
Casasnovas J M, Bickford J K, Springer T A
机构信息
The Center for Blood Research and Harvard Medical School Department of Pathology, Boston, Massachusetts 02115, USA.
出版信息
J Virol. 1998 Jul;72(7):6244-6. doi: 10.1128/JVI.72.7.6244-6246.1998.
Abstract
Fragments of intercellular adhesion molecule 1 (ICAM- 1) containing only the two most N terminal of its five immunoglobulin SF domains bind to rhinovirus 3 with the same affinity and kinetics as a fragment with the entire extracellular domain. The fully active two-domain fragments contain 5 or 14 more residues than a previously described fragment that is only partially active. Comparison of X-ray crystal structures show differences at the bottom of domain 2. Four different glycoforms of ICAM- 1 bind with identical kinetics.
摘要
仅包含其五个免疫球蛋白超家族（SF）结构域中最靠近N端的两个结构域的细胞间粘附分子1（ICAM-1）片段，与鼻病毒3的结合亲和力和动力学与具有完整细胞外结构域的片段相同。完全活性的双结构域片段比先前描述的仅部分活性的片段多5个或14个残基。X射线晶体结构比较显示结构域2底部存在差异。ICAM-1的四种不同糖型以相同的动力学结合。
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The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand.人细胞间黏附分子-1（ICAM-1）两个氨基末端结构域的结构揭示了其作为鼻病毒受体和淋巴细胞功能相关抗原-1（LFA-1）整合素配体的作用机制。
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