Solution NMR structure of a sheddase inhibitor prodomain from the malarial parasite Plasmodium falciparum.

Solution NMR structure of a sheddase inhibitor prodomain from the malarial parasite Plasmodium falciparum.
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疟疾寄生虫恶性疟原虫脱落酶抑制剂前结构域的溶液核磁共振结构。

DOI:
10.1002/prot.24187
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发表时间:
2012
期刊:
影响因子:
2.9
通讯作者:
Orban,John
Orban,John
中科院分区:
生物学4区
文献类型:
--
作者:
He,Yanan;Chen,Yihong;Oganesyan,Natalia;Ruan,Biao;O'Brochta,David;Bryan,PhilipN;Orban,John

文献摘要

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Plasmodium subtilisin 2 (Sub2) 是一种多域蛋白,在疟疾感染中发挥重要作用。在这里,我们描述了恶性疟原虫 Sub2 抑制性前结构域保守区域(称为 prosub2)的溶液 NMR 结构。尽管不存在任何可检测到的序列同源性,原生动物 prosub2 与细菌和哺乳动物枯草杆菌蛋白酶样前结构域具有结构相似性。与这些其他前结构域的三维结构的比较表明,可能存在与 Sub2 催化结构域的结合界面,并提供了对疟原虫前结构域中初级和次级加工位点位置的见解。蛋白质2012;。 © 2012 Wiley 期刊公司。
Plasmodiumsubtilisin 2 (Sub2) is a multidomain protein that plays an important role in malaria infection. Here, we describe the solution NMR structure of a conserved region of the inhibitory prodomain of Sub2 fromPlasmodium falciparum, termed prosub2. Despite the absence of any detectable sequence homology, the protozoan prosub2 has structural similarity to bacterial and mammalian subtilisin‐like prodomains. Comparison with the three‐dimensional structures of these other prodomains suggests a likely binding interface with the catalytic domain of Sub2 and provides insights into the locations of primary and secondary processing sites inPlasmodiumprodomains. Proteins 2012;. © 2012 Wiley Periodicals, Inc.