Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains.
Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains.
复制标题
大鼠 CD4 结构域 3 和 4 的晶体结构：与 NH2 末端结构域的关系。
作者：
R. L. Brady;Eleanor J. Dodson;Guy Dodson;G. Lange;S. Davis;Alan F. Williams;A. Barclay
CD4抗原是T淋巴细胞的膜糖蛋白，与主要组织相容性复合体II类抗原相互作用，也是人类免疫缺陷病毒的受体。 CD4 的胞外部分预计会折叠成四个免疫球蛋白样结构域。以 2.8 埃分辨率解析了大鼠 CD4 第三和第四结构域的晶体结构，并显示这两个结构域都具有免疫球蛋白折叠。然而，结构域 3 缺乏 β 片层之间的二硫键；这导致域的扩展。与结构域 1 和 2 相比，结构域 3 和结构域 4 之间的方向存在 30 度的差异。两个 CD4 片段结构为提出整体受体模型提供了基础。这些模型提出了一种延伸结构，包括由短且可能柔性的接头区域连接的两个刚性部分。
The CD4 antigen is a membrane glycoprotein of T lymphocytes that interacts with major histocompatibility complex class II antigens and is also a receptor for the human immunodeficiency virus. the extracellular portion of CD4 is predicted to fold into four immunoglobulin-like domains. The crystal structure of the third and fourth domains of rat CD4 was solved at 2.8 angstrom resolution and shows that both domains have immunoglobulin folds. Domain 3, however, lacks the disulfide between the beta sheets; this results in an expansion of the domain. There is a difference of 30 degrees in the orientation between domains 3 and 4 when compared with domains 1 and 2. The two CD4 fragment structures provide a basis from which models of the overall receptor can be proposed. These models suggest an extended structure comprising two rigid portions joined by a short and possibly flexible linker region.
影响因子：
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作者：
PARNES, JR
通讯作者：
PARNES, JR