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首页> 外文期刊>Clinical immunology: The official journal of the Clinical Immunology Society >Structural relationship of lambda-type light chains with AL amyloidosis.
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Structural relationship of lambda-type light chains with AL amyloidosis.

机译：λ型轻链与AL淀粉样变性的结构关系。

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摘要

Three human amyloidogenic Bence Jones proteins, NIG76 VlambdaII, NIG204 VlambdaI, and NIG250 VlambdaV, were characterized. In a comparative study, three amino acids, Ser-25a, Thr-68, and Val-95, were found to be common to amyloidogenic proteins of the VlambdaII subgroup. NIG204 had an insertion of Pro residue following position 30 (30a). Proteins having an insertion at this position are invariantly amyloidogenic. NIG250 had a characteristic VlambdaV VL domain, with Mcg+ and KERN+ CL domain isotypes. Following the protein DEL, this is the second example of this subgroup. No common residue is found in the other subgroup proteins but unique substitutions do occur. It would seem that any substitution that causes an alteration in the protein conformation may lead to its being more prone to association with the amyloid processes. Copyright 1999 Academic Press.
机译：表征了三种人类淀粉样蛋白生成的Bence Jones蛋白，分别为NIG76 VlambdaII，NIG204 VlambdaI和NIG250 VlambdaV。在一项比较研究中，发现三个氨基酸Ser-25a，Thr-68和Val-95是VlambdaII亚组的淀粉样蛋白共同的蛋白质。 NIG204在位置30（30a）之后插入Pro残基。在该位置具有插入的蛋白质始终是淀粉样蛋白。 NIG250具有特征性的VlambdaV VL结构域，具有Mcg +和KERN + CL结构域同种型。继蛋白质DEL之后，这是该亚组的第二个例子。在其他亚组蛋白中未发现常见残基，但确实发生了独特的取代。似乎任何引起蛋白质构象改变的取代都可能导致其更易于与淀粉样蛋白结合。版权所有1999，学术出版社。

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