水通道蛋白
恶性疟原虫
寄生虫寄主
水通道蛋白1
生物
生物化学
疟原虫(生命周期)
化学
生物物理学
疟疾
水道
万维网
工程类
机械工程
入口
免疫学
计算机科学
作者
Zachary E. Newby,Joseph D. O’Connell,Yaneth Robles-Colmenares,Shahram Khademi,Larry J. W. Miercke,Robert M. Stroud
摘要
The 2.05-A resolution structure of the aquaglyceroporin from the malarial parasite Plasmodium falciparum (PfAQP), a protein important in the parasite's life cycle, has been solved. The structure provides key evidence for the basis of water versus glycerol selectivity in aquaporin family members. Unlike its closest homolog of known structure, GlpF, the channel conducts both glycerol and water at high rates, framing the question of what determines high water conductance in aquaporin channels. The universally conserved arginine in the selectivity filter is constrained by only two hydrogen bonds in GlpF, whereas there are three in all water-selective aquaporins and in PfAQP. The decreased cost of dehydrating the triply-satisfied arginine cation may provide the basis for high water conductance. The two Asn-Pro-Ala (NPA) regions of PfAQP, which bear rare substitutions to Asn-Leu-Ala (NLA) and Asn-Pro-Ser (NPS), participate in preserving the orientation of the selectivity filter asparagines in the center of the channel.
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