首页> 外文期刊>FEBS Letters >Hydrophobie cluster analysis reveals duplication in the external structure of human α‐interferon receptor and homology with γ‐interferon receptor external domain
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Hydrophobie cluster analysis reveals duplication in the external structure of human α‐interferon receptor and homology with γ‐interferon receptor external domain

机译:疏水性聚类分析揭示了人类α-干扰素受体的外部结构重复以及与γ-干扰素受体外部结构域的同源性

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摘要

>Evidence is presented, based on sequence comparison according to Hydrophobic Cluster Analysis, of a structural and evolutionary relationship between the human α/β-interferon receptor and the human and mouse γ-interferon receptor. These results predict that the human α/β-interferon receptor extracellular part is organised in two homologous subdomains connected by a proline linker. They also predict that both subdomains present some homologies to the external domain of mouse and human γ interferon receptor.
机译:通过基于疏水聚类分析的序列比较,提供了人类α/β-干扰素受体与人类和小鼠γ-干扰素受体之间的结构和进化关系的证据。这些结果预示人α/β-干扰素受体胞外部分被组织在两个脯氨酸连接子连接的同源亚域中。他们还预测这两个亚结构域与小鼠和人类γ干扰素受体的外部结构域呈现出某些同源性。

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