Leukocyte cell-derived chemotaxin 2 is a zinc-binding protein
Leukocyte cell-derived chemotaxin 2 is a zinc-binding protein
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DOI：
10.1016/j.febslet.2013.01.025
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发表时间：
2013-03-01
期刊：
影响因子：
3.5
通讯作者：
Yamagoe, Satoshi
中科院分区：
文献类型：
--
作者：
Okumura, Akinori;Suzuki, Takehiro;Yamagoe, Satoshi
白细胞源性趋化因子 2 (LECT2) 是一种分泌性肝蛋白，与多种生理活性相关。 LECT2 属于肽酶 M23 家族，表明它是一种锌结合蛋白。为了测试这种可能性，进行了电喷雾电离质谱和 X 射线吸收精细结构分析。这些实验的结果表明，由动物细胞系产生的重组小鼠LECT2含有锌原子。此外，发现重组LECT2在体外通过二硫键自我寡聚化，但是通过添加锌来抑制这种现象。这些结果表明锌稳定了 LECT2 结构。蛋白质相互作用的结构化摘要：LECT2 和 LECT2 通过交联研究结合（查看相互作用）LECT2 和 LECT2 通过凝胶电泳中的共迁移结合（查看相互作用）LECT2 和 LECT2 通过凝胶电泳中的共迁移结合（查看相互作用：1、2、3）LECT2 和 LECT2 通过交联研究结合（查看相互作用：1、 2, 3)LECT2 和 LECT2 在凝胶电泳中通过共迁移结合（查看相互作用：1,2,3） (C) 2013 年欧洲生化协会联合会。由 Elsevier B.V. 出版。保留所有权利。
Leukocyte cell-derived chemotaxin 2 (LECT2) is a secreted hepatic protein that has been associated with several physiological activities. LECT2 belongs to the peptidase M23 family, suggesting that it is a zinc-binding protein. To test this possibility, electrospray ionization mass spectrometry and X-ray absorption fine-structure analysis were performed. Results of these experiments indicated that recombinant mouse LECT2 produced by an animal cell line contains a zinc atom. Furthermore, the recombinant LECT2 was found to be self-oligomerized by disulfide bonds in vitro, but this was suppressed by addition of zinc. These results indicated that zinc stabilizes the LECT2 structure.Structured summary of protein interactions:LECT2 and LECT2 bind by cross-linking study (View interaction)LECT2 and LECT2 bind by comigration in gel electrophoresis (View interaction)LECT2 and LECT2 bind by comigration in gel electrophoresis (View interaction: 1, 2, 3)LECT2 and LECT2 bind by cross-linking study (View interaction: 1, 2, 3)LECT2 and LECT2 bind by comigration in gel electrophoresis (View interaction: 1, 2, 3) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.