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Structural Research of APC Superfamily

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The amino acid/polyamine/organocation (APC) superfamily encompasses a diverse group of transmembrane transporters involved in the transport of small organic molecules such as amino acids, polyamines, and ions across the lipid bilayer. This superfamily is crucial for maintaining cellular homeostasis and is involved in many physiological processes, including nutrient uptake, ion homeostasis, and signaling.

Crystallography and cryo-electron microscopy have been used to determine the three-dimensional structures of various APC transporters, providing a detailed view of the transport mechanism. NKCC1 protein is a cation-chloride cotransporter involved in the transport of ions across cell membranes. The molecular structure of the protein has been determined, including its transmembrane domains and regulatory regions, and how it interacts with ions and other molecules. NKCC1 can transport ions across membranes through various mechanisms, including through the use of sodium-potassium pumps and the action of various transport proteins and channels. These studies suggest that a better understanding of the structure and mechanism of NKCC1 may lead to the development of new therapies for conditions such as hypertension and epilepsy, which are associated with the dysregulation of ion transport.

Overall structure of NKCC1 dimerFigure 1. Overall structure of NKCC1 dimer. (Chew T A, et al., 2019)

ProteinOrganismMethodResolutionPDB Entry ID
Arginine Agmatine Antiporter (AdiC) (expressed in E. coli)Escherichia coliX-ray diffraction3.61 Å3LRB
AdiC (N22A, L123W mutant) with bound Arginine (expressed in E. coli)Escherichia coliX-ray diffraction3.00 Å3L1L
AdiC (N101A) in the open-to-out Arg+ bound conformation (expressed in E. coli)Escherichia coliX-ray diffraction3.00 Å3OB6
AdiC in complex with agmatine (expressed in E. coli)Escherichia coliX-ray diffraction2.59 Å5J4N
AdiC, outward open substrate-free state (expressed in E. coli)Escherichia coliX-ray diffraction1.69 Å7O82
AdiC in complex with a Fab fragment (expressed in E. coli)Salmonella entericaX-ray diffraction3.20 Å3NCY
ApcT Transporter (expressed in E. coli)Methanocaldococcus jannaschiiX-ray diffraction2.32 Å3GIA
Glutamate-GABA antiporter GadC (expressed in E. coli)Escherichia coliX-ray diffraction3.10 Å4DJK
AgcS sodium/alanine symporter with bound L-alanine (expressed in E. coli)Methanococcus maripaludisX-ray diffraction3.24 Å6CSE
BasC alanine-serine-cysteine exchanger, open-inward conformation (expressed in E. coli)Carnobacterium sp. AT7X-ray diffraction2.92 Å6F2G
NKCC1 TM domain (expressed in Spodoptera frugiperda)Danio rerioCryo-EM single particle analysis2.90 Å6NPH
NKCC1 cation-chloride cotransporter (CCC), partially loaded, inward open state (expressed in Spodoptera frugiperda)Homo sapiensCryo-EM single particle analysis3.46 Å6PZT
KCC1 cation-chloride cotransporter (CCC) in glyo-diosgenin (GDN) detergent, 150 mM KCl (expressed in HEK293 cells)Homo sapiensCryo-EM single particle analysis2.90 Å6KKR
KCC1 Δ19 cation-chloride cotransporter (CCC) in NaCl (expressed in HEK293 cells)Homo sapiensCryo-EM single particle analysis3.12 Å7AIP
KCC1 cation-chloride cotransporter (CCC) with bound VU0463271, outward-open state (expressed in HEK293 cells)Homo sapiensCryo-EM single particle analysis3.50 Å7TTI
KCC3 cation-chloride cotransporter (CCC) (expressed in HEK293 cells)Homo sapiensCryo-EM single particle analysis3.60 Å7D90
KCC3b cation-chloride cotransporter (CCC), wild-type in NaCl (expressed in HEK293 cells)Homo sapiensCryo-EM single particle analysis3.64 Å7NGB
KCC4 cation-chloride cotransporter (CCC) (expressed in HEK293 cells)Homo sapiensCryo-EM single particle analysis2.90 Å7D99
KCC4 cation-chloride cotransporter (CCC) in nanodiscs (expressed in Sf9 cells)Mus musculusCryo-EM single particle analysis3.65 Å6UKN
KimA K+/H+ symporter, inward-facing occluded state (expressed in E. coli)Bacillus subtilisCryo-EM single particle analysis3.70 Å6S3K

Table 1. Structural Research of Amino Acid/Polyamine/Organocation (APC) Superfamily.

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References

  1. Chew T A, et al. Structure and mechanism of the cation-chloride cotransporter NKCC1. Nature. 2019, 572(7770): 488-492.
  2. Zhao Y, et al. Structure of the human cation-chloride cotransport KCC1 in an outward-open state. Proceedings of the National Academy of Sciences. 2022, 119(27): e2109083119.

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