Effects of amino acid mutations in the pore-forming domain of the hemolytic lectin CEL-III
Effects of amino acid mutations in the pore-forming domain of the hemolytic lectin CEL-III
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溶血凝集素 CEL-III 成孔结构域氨基酸突变的影响
DOI：
10.1080/09168451.2016.1176520
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发表时间：
2016
期刊：
影响因子：
--
通讯作者：
Tomomitsu Hatakeyama
中科院分区：
文献类型：
--
作者：
Tomonao Nagao;Risa Masaki;Hideaki Unno;Shuichiro Goda;Tomomitsu Hatakeyama
溶血性凝集素CEL-III在靶细胞的膜中形成跨膜孔。对CEL-III结构域3中Lys 405位点定向突变的影响的研究表明，该残基被相对较小的残基取代导致溶血活性显著增加，表明适度去稳定化结构域3通过构象变化促进跨膜孔的形成。
The hemolytic lectin CEL-III forms transmembrane pores in the membranes of target cells. A study on the effect of site-directed mutation at Lys405 in domain 3 of CEL-III indicated that replacements of this residue by relatively smaller residues lead to a marked increase in hemolytic activity, suggesting that moderately destabilizing domain 3 facilitates formation of transmembrane pores through conformational changes.