含有不同寻常的天冬酰胺-脯氨酸-丙氨酸（NPA）模体的水通道蛋白-11具有正常的水通道活性。
Aquaporin-11 containing a divergent NPA motif has normal water channel activity.
作者信息
Yakata Kaya, Hiroaki Yoko, Ishibashi Kenichi, Sohara Eisei, Sasaki Sei, Mitsuoka Kaoru, Fujiyoshi Yoshinori
机构信息
Department of Biophysics, Faculty of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku Kyoto 606-8502, Japan.
出版信息
Biochim Biophys Acta. 2007 Mar;1768(3):688-93. doi: 10.1016/j.bbamem.2006.11.005. Epub 2006 Nov 11.
Recently, two novel mammalian aquaporins (AQPs), AQPs 11 and 12, have been identified and classified as members of a new AQP subfamily, the "subcellular AQPs". In members of this subfamily one of the two asparagine-proline-alanine (NPA) motifs, which play a crucial role in selective water conduction, are not completely conserved. Mouse AQP11 (mAQP11) was expressed in Sf9 cells and purified using the detergent Fos-choline 10. The protein was reconstituted into liposomes, which were used for water conduction studies with a stopped-flow device. Single water permeability (pf) of AQP11 was measured to be 1.72+/-0.03x10(-13) cm(3)/s, suggesting that other members of the subfamily with incompletely conserved NPA motifs may also function as water channels.
最近，两种新的哺乳动物水通道蛋白（AQP），即AQP11和AQP12，已被鉴定并归类为一个新的AQP亚家族“亚细胞AQP”的成员。在该亚家族成员中，对选择性水传导起关键作用的两个天冬酰胺-脯氨酸-丙氨酸（NPA）基序之一并不完全保守。小鼠AQP11（mAQP11）在Sf9细胞中表达，并使用去污剂福斯-胆碱10进行纯化。该蛋白被重组到脂质体中，脂质体用于通过停流装置进行水传导研究。AQP11的单水渗透率（pf）测得为1.72±0.03×10（-13）cm³/s，这表明具有不完全保守NPA基序的该亚家族其他成员也可能作为水通道发挥作用。
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