免疫球蛋白G1第290位残基对其SH2结构域的结构和生物学特性的影响
[Effect of immunoglobulin G1 Pro 290 residue on structural and biological characteristics of its SH2 domain].
作者信息
Tishchenko V M
机构信息
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, Russia.
出版信息
Bioorg Khim. 1998 Jun;24(6):465-7.
PMID:9702356
Abstract
Tryptic hydrolysis of only one of 11 studied Fc fragments of human myeloma immunoglobulins G1 (IgG1) provided an intact CH2 domain in a high yield (up to 40% as opposed to 2-3% for other IgG1s). The only structural difference of this domain was shown to be the substitution of Pro for Lys290. This decreased the capacity of the IgG1 Sem Fc fragment to interact with proteins of the complement system.
摘要
对11种研究的人骨髓瘤免疫球蛋白G1（IgG1）Fc片段中的仅一种进行胰蛋白酶水解，可高产量地提供完整的CH2结构域（高达40%，而其他IgG1s为2-3%）。该结构域唯一的结构差异显示为Pro替代了Lys290。这降低了IgG1 Sem Fc片段与补体系统蛋白质相互作用的能力。
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