The SLC6/NSS family members KAAT1 and CAATCH1 have a weak chloride dependence
Autor: | V. F. Sacchi, Antonio Peres, Michela Castagna, Elena Bossi, Sara Bettè |
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Rok vydání: | 2008 |
Předmět: |
GABA Plasma Membrane Transport Proteins
Biophysics ION-BINDING NA+ RAT-BRAIN Biochemistry Chlorides Manduca Leucine binding Glutamate aspartate transporter Animals GABA transporter Amines Amino Acids COTRANSPORTER KAAT1 Serotonin transporter GAMMA-AMINOBUTYRIC-ACID Dopamine transporter chemistry.chemical_classification Neurotransmitter Agents biology XENOPUS OOCYTES GABA TRANSPORTER Membrane Proteins Biological Transport Transporter CHLORINE DEPENDENCE Amino acid SODIUM Amino Acid Transport Systems Neutral chemistry SELECTIVITY GAT1 GAMMA-AMINOBUTYRIC-ACID GABA TRANSPORTER RAT-BRAIN COTRANSPORTER KAAT1 XENOPUS OOCYTES ION-BINDING NA+ SELECTIVITY SODIUM GAT1 Symporter biology.protein Insect Proteins Carrier Proteins |
Zdroj: | ResearcherID |
Popis: | KAAT1 and CAATCH1 are amino acid transporters cloned from the intestine of the lepidoptera Manduca sexta.1,2 They are members of the SLC6/NSS family, which groups membrane proteins that use Na+, K+, and Cl- gradients for the coupled transport of amines and amino acids. The report of the atomic-resolution x-ray crystal structure of the eubacterium Aquifex aeolicus leucine transporter (AaLeuT)3 has contributed significantly to understanding of the structure–function relationship in NSS proteins. Transport by AaLeuT is Cl- independent, whereas many neurotransmitter:sodium symporters like serotonin transporter (SERT), GABA transporter (GAT1), dopamine transporter, and norephinephrine transporter, among others, are strongly Cl- dependent.4 A single Cl- ion is found bound to one of the extracellular loops, EL2 in AaLeuT. The Cl- is 20 A… away from the Na and leucine binding sites, and thus it is unclear whether this Cl- binding site is physiologically important. The nature of the association of Cl- ions with ... |
Databáze: | OpenAIRE |
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