Leave a Message
My Cart ()
Inquiry Basket
Contact Us

Structural Research of Aquaporins and Glyceroporins

Inquiry

Aquaporins and glyceroporins are a class of transmembrane proteins that serve as gatekeepers for the transport of water and glycerol across cell membranes. These proteins have a critical role in regulating the water and energy balance within the body, and their dysfunction has been linked to an array of diseases, ranging from diabetes to kidney disorders.

The structure of aquaporin-1 (AQP1) was first determined in 1994, illuminating a water-selective channel that allows the rapid transport of water molecules across the membrane. A recent study used X-ray crystallography to determine the structure of human aquaglyceroporin AQP7 in complex with glycerol. The results revealed that AQP7 has a distinct architecture that grants it the ability to selectively transport glycerol, while simultaneously excluding other solutes. The study also found that AQP7 undergoes conformational changes during glycerol transport, which further reinforces its high selectivity. The structure of AQP7 has since been used as a template for the determination of the structures of other glyceroporins, such as AQP3 and AQP9.

The overall structure of human AQP7.Figure 1. The overall structure of human AQP7. (de Mare S W, et al., 2020)

ProteinOrganismMethodResolutionPDB Entry ID
AQP0 aquaporin water channelBos taurusX-ray diffraction2.24 Å1YMG
AQP0 aquaporin water channel from sheep lensOvis ariesElectron crystallography3.00 Å1SOR
AQP0 aquaporin sheep lens junctionOvis ariesElectron crystallography1.90 Å2B6O
AQP0 aquaporin sheep lens junction in E. coli polar lipidsOvis ariesElectron crystallography2.50 Å3M9I
AQP1 red blood cell aquaporin water channelHomo sapiensElectron crystallography3.80 Å1FQY
AQP1 red blood cell aquaporin water channelHomo sapiensElectron crystallography3.70 Å1IH5
AQP1 red blood cell aquaporin water channel (expressed in Spodoptera frugiperda)Homo sapiensX-ray diffraction3.28 Å4CSK
AQP1 red blood cell aquaporin water channel (expressed in Komagataella pastoris)Homo sapiensSolid-state NMR/6POJ
AQP1 aquaporin red blood cell water channelBos taurusX-ray diffraction2.20 Å1J4N
AQP2 Aquaporin from kidney (expressed in Komagataella phaffii)Homo sapiensX-ray diffraction2.75 Å4NEF
AQP2 Aquaporin from kidney crystallized on a silicon chip (expressed in Komagataella phaffii)Homo sapiensX-ray diffraction3.70 Å6QF5
AQP4 aquaporin rat glial cell water channel (expressed in Spodoptera frugiperda)Rattus norvegicusElectron crystallography3.70 Å2D57
AQP4 aquaporin rat glial cell water channel (expressed in Spodoptera frugiperda)Rattus norvegicusElectron crystallography2.80 Å2ZZ9
AQP4 aquaporin water channel (expressed in Komagataella pastoris)Homo sapiensX-ray diffraction1.80 Å3GD8
Aquaporin 5 (AQP5) (expressed in Komagataella pastoris)Homo sapiensX-ray diffraction2.00 Å3D9S
Aquaporin 7 (expressed in Komagataella pastoris)Homo sapiensX-ray diffraction1.90 Å6QZI
AQP7 dimer of tetramers_D4 (expressed in Komagataella pastoris)Homo sapiensCryo-EM single particle analysis2.55 Å8AMX
AQP10 (expressed in Saccharomyces cerevisiae)Homo sapiensX-ray diffraction2.30 Å6F7H
AqpM aquaporin water channel (expressed in E. coli)Methanothermobacter marburgensisX-ray diffraction1.68 Å2F2B
Aquaporin Z (expressed in E. coli)Escherichia coliX-ray diffraction2.50 Å1RC2
AqpZ aquaporin showing two conformations of Arg-189 (expressed in E. coli)Escherichia coliX-ray diffraction3.20 Å2ABM
AqpZ aquaporin (C9S/C20S), T183C mutant without Hg (expressed in E. coli)Escherichia coliX-ray diffraction2.30 Å2O9D
AqpZ mutant F43W (expressed in E. coli)Escherichia coliX-ray diffraction2.40 Å3NK5
PIP2;1 plant aquaporin (closed conformation) (expressed in Komagataella pastoris)Spinacia oleraceaX-ray diffraction2.10 Å1Z98
PIP2;1 plant aquaporin, S115E mutant (expressed in Komagataella pastoris)Spinacia oleraceaX-ray diffraction2.30 Å3CLL
PIP2;4 plant aquaporin (expressed in Komagataella pastoris)Arabidopsis thalianaX-ray diffraction3.70 Å6QIM
TIP2;1 ammonia-permeable aquaporin (expressed in Komagataella pastoris)Arabidopsis thalianaX-ray diffraction1.18 Å5I32
GlpF glycerol facilitator channel (expressed in E. coli)Escherichia coliX-ray diffraction2.20 Å1FX8
GlpF glycerol facilitator channel, W84F/F200T-mutant (expressed in E. coli)Escherichia coliX-ray diffraction2.10 Å1LDF
AQP aquaglyceroporin (expressed in E. coli)Plasmodium falciparumX-ray diffraction2.05 Å3C02
Aqy1 yeast aquaporin (pH 3.5)Komagataella pastorisX-ray diffraction1.15 Å2W2E
Aqy1 yeast aquaporin (pH 8.0) (expressed in Komagataella pastoris)Komagataella pastorisX-ray diffraction0.88 Å3ZOJ
NIP2;1 aquaporin (metalloid porin) silicon transporter (expressed in Saccharomyces cerevisiae)Oryza sativaX-ray diffraction3.00 Å7NL4
Lsi1 aquaporin (metalloid porin) silicon transporter (expressed in Spodoptera frugiperda)Oryza sativaX-ray diffraction1.80 Å7CJS

Table 1. Structural Research of Aquaporins and Glyceroporins.

At Creative Biostructure, we have a team of experts with extensive experience in the structural analysis of proteins, including aquaporins and glyceroporins. We use cutting-edge techniques to determine the structure of these proteins at high resolution, providing insights into their function and potential therapeutic applications.

Our services include X-ray crystallography, cryo-electron microscopy, and nuclear magnetic resonance spectroscopy, allowing us to provide our clients with a comprehensive structural analysis of their proteins. We work closely with our clients to ensure that our services meet their specific research needs, and we provide detailed reports and analyses to help them interpret the results. If you are interested in learning more about our services, please do not hesitate to contact us directly. Our team of experts is always available to discuss your research needs and provide you with the best possible solutions.

References

  1. de Mare S W, et al. Structural basis for glycerol efflux and selectivity of human aquaporin 7. Structure. 2020, 28(2): 215-222. e3.
  2. Saitoh Y, et al. Structural basis for high selectivity of a rice silicon channel Lsi1. Nature Communications. 2021, 12(1): 6236.
  3. Huang P, et al. Cryo-EM structure supports a role of AQP7 as a junction protein. Nature Communications. 2023, 14(1): 600.
OUR VALUED PARTNERSHIPS
mit harvard stanford nih abbvie novartis amgen gsk regeneron sanofi

Online Inquiry

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Inquiry
back to top
Advertisement Learn More