메뉴 건너뛰기




Volumn 385, Issue 2, 2009, Pages 210-214

Substrate-Na+ complex formation: Coupling mechanism for γ-aminobutyrate symporters

Author keywords

Charge assisted hydrogen bonding; Glial subtypes of human aminobutyric acid transporters; Homology modeling; Molecular dynamics; Neurotransmitter sodium symporters; Substrate docking; Substrate Na+ ion complex; Zinc ion

Indexed keywords

4 AMINOBUTYRIC ACID; 4 AMINOBUTYRIC ACID CARRIER; AMPHOLYTE; SODIUM ION; ZINC ION;

EID: 67349216187     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.05.040     Document Type: Article
Times cited : (10)

References (38)
  • 2
    • 58149230945 scopus 로고    scopus 로고
    • Biochemistry, an almost-complete movie
    • Diallinas G. Biochemistry, an almost-complete movie. Science 322 (2008) 1644-1645
    • (2008) Science , vol.322 , pp. 1644-1645
    • Diallinas, G.1
  • 4
    • 61449361479 scopus 로고    scopus 로고
    • The molecular logic of sodium-coupled neurotransmitter transporters
    • Gouaux E. The molecular logic of sodium-coupled neurotransmitter transporters. Philos. Trans. R. Soc. Lond. B Biol. Sci. 364 (2009) 149-154
    • (2009) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.364 , pp. 149-154
    • Gouaux, E.1
  • 5
    • 58149233796 scopus 로고    scopus 로고
    • A competitive inhibitor traps LeuT in an open-to-out conformation
    • Singh S.K., Piscitelli C.L., Yamashita A., and Gouaux E. A competitive inhibitor traps LeuT in an open-to-out conformation. Science 322 (2008) 1655-1661
    • (2008) Science , vol.322 , pp. 1655-1661
    • Singh, S.K.1    Piscitelli, C.L.2    Yamashita, A.3    Gouaux, E.4
  • 6
    • 34548178234 scopus 로고    scopus 로고
    • Antidepressant binding site in a bacterial homologue of neurotransmitter transporters
    • Singh S.K., Yamashita A., and Gouaux E. Antidepressant binding site in a bacterial homologue of neurotransmitter transporters. Nature 448 (2007) 952-956
    • (2007) Nature , vol.448 , pp. 952-956
    • Singh, S.K.1    Yamashita, A.2    Gouaux, E.3
  • 8
    • 34548684744 scopus 로고    scopus 로고
    • LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake
    • Zhou Z., Zhen J., Karpowich N.K., Goetz R.M., Law C.J., Reith M.E.A., and Wang D. LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake. Science 317 (2007) 1390-1393
    • (2007) Science , vol.317 , pp. 1390-1393
    • Zhou, Z.1    Zhen, J.2    Karpowich, N.K.3    Goetz, R.M.4    Law, C.J.5    Reith, M.E.A.6    Wang, D.7
  • 9
    • 0242660375 scopus 로고    scopus 로고
    • Inhibition of gamma-aminobutyric acid uptake: anatomy, physiology and effects against epileptic seizures
    • Dalby N.O. Inhibition of gamma-aminobutyric acid uptake: anatomy, physiology and effects against epileptic seizures. Eur. J. Pharmacol. 479 (2003) 127-137
    • (2003) Eur. J. Pharmacol. , vol.479 , pp. 127-137
    • Dalby, N.O.1
  • 10
    • 33744486599 scopus 로고    scopus 로고
    • Role for GABA and Glu plasma membrane transporters in the interplay of inhibitory and excitatory neurotransmission
    • Héja L., Karacs K., and Kardos J. Role for GABA and Glu plasma membrane transporters in the interplay of inhibitory and excitatory neurotransmission. Curr. Top. Med. Chem. 6 (2006) 989-995
    • (2006) Curr. Top. Med. Chem. , vol.6 , pp. 989-995
    • Héja, L.1    Karacs, K.2    Kardos, J.3
  • 11
    • 44849091207 scopus 로고    scopus 로고
    • Sodium-coupled neurotransmitter transporters
    • Kanner B.I., and Zomot E. Sodium-coupled neurotransmitter transporters. Chem. Rev. 108 (2008) 1654-1668
    • (2008) Chem. Rev. , vol.108 , pp. 1654-1668
    • Kanner, B.I.1    Zomot, E.2
  • 14
    • 0027391644 scopus 로고
    • Molecular characterization of four pharmacologically distinct gamma-aminobutyric acid transporters in mouse brain
    • Liu Q.R., López-Corcuera B., Mandiyan S., Nelson H., and Nelson N. Molecular characterization of four pharmacologically distinct gamma-aminobutyric acid transporters in mouse brain. J. Biol. Chem. 268 (1993) 2106-2112
    • (1993) J. Biol. Chem. , vol.268 , pp. 2106-2112
    • Liu, Q.R.1    López-Corcuera, B.2    Mandiyan, S.3    Nelson, H.4    Nelson, N.5
  • 15
    • 17844394176 scopus 로고    scopus 로고
    • Zinc inhibition of γ-aminobutyric acid transporter 4 (GAT4) reveals a link between excitatory and inhibitory neurotransmission
    • Cohen-Kfir E., Lee W., Eskandari S., and Nelson N. Zinc inhibition of γ-aminobutyric acid transporter 4 (GAT4) reveals a link between excitatory and inhibitory neurotransmission. Proc. Natl. Acad. Sci. USA 102 (2005) 6154-6159
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6154-6159
    • Cohen-Kfir, E.1    Lee, W.2    Eskandari, S.3    Nelson, N.4
  • 16
    • 33644908284 scopus 로고    scopus 로고
    • Functional characterization of Zn2+-sensitive GABA transporter expressed in primary cultures of astrocytes from rat cerebral cortex
    • Wu Q., Wada M., Shimada A., Yamamoto A., and Fujita T. Functional characterization of Zn2+-sensitive GABA transporter expressed in primary cultures of astrocytes from rat cerebral cortex. Brain Res. 1075 (2006) 100-109
    • (2006) Brain Res. , vol.1075 , pp. 100-109
    • Wu, Q.1    Wada, M.2    Shimada, A.3    Yamamoto, A.4    Fujita, T.5
  • 17
    • 0033601168 scopus 로고    scopus 로고
    • Defining proximity relationships in the tertiary structure of the dopamine transporter, identification of a conserved glutamic acid as a third coordinate in the endogenous Zn2+-binding site
    • Loland C.J., Norregaard L., and Gether U. Defining proximity relationships in the tertiary structure of the dopamine transporter, identification of a conserved glutamic acid as a third coordinate in the endogenous Zn2+-binding site. J. Biol. Chem. 274 (1999) 36928-36934
    • (1999) J. Biol. Chem. , vol.274 , pp. 36928-36934
    • Loland, C.J.1    Norregaard, L.2    Gether, U.3
  • 20
    • 34447637751 scopus 로고    scopus 로고
    • Discontinuous membrane helices in transport proteins and their correlation with function
    • Screpanti E., and Hunte C. Discontinuous membrane helices in transport proteins and their correlation with function. J. Struct. Biol. 159 (2007) 261-267
    • (2007) J. Struct. Biol. , vol.159 , pp. 261-267
    • Screpanti, E.1    Hunte, C.2
  • 22
    • 40649098564 scopus 로고    scopus 로고
    • + binding sites with two different mechanisms
    • + binding sites with two different mechanisms. J. Mol. Biol. 377 (2008) 804-818
    • (2008) J. Mol. Biol. , vol.377 , pp. 804-818
    • Noskov, S.Y.1    Roux, B.2
  • 23
    • 41449093586 scopus 로고    scopus 로고
    • Substrate binding and formation of an occluded state in the leucine transporter
    • Celik L., Schiøtt B., and Tajkhorshid E. Substrate binding and formation of an occluded state in the leucine transporter. Biophys. J. 94 (2008) 1600-1612
    • (2008) Biophys. J. , vol.94 , pp. 1600-1612
    • Celik, L.1    Schiøtt, B.2    Tajkhorshid, E.3
  • 24
    • 33751194447 scopus 로고    scopus 로고
    • + symporters (NSS) aids in the use of the LeuT structure to probe NSS structure and function
    • + symporters (NSS) aids in the use of the LeuT structure to probe NSS structure and function. Mol. Pharmacol. 70 (2006) 1630-1642
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1630-1642
    • Beuming, T.1    Shi, L.2    Javitch, J.A.3    Weinstein, H.4
  • 25
    • 34547118847 scopus 로고    scopus 로고
    • Cloning and characterization of a functional human γ-aminobutyric acid (GABA) transporter, human GAT-2
    • Christiansen B., Meinild A., Jensen A.A., and Bräuner-Osborne H. Cloning and characterization of a functional human γ-aminobutyric acid (GABA) transporter, human GAT-2. J. Biol. Chem. 282 (2007) 19331-19341
    • (2007) J. Biol. Chem. , vol.282 , pp. 19331-19341
    • Christiansen, B.1    Meinild, A.2    Jensen, A.A.3    Bräuner-Osborne, H.4
  • 26
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL repository of annotated three-dimensional protein structure homology models
    • Kopp J., and Schwede T. The SWISS-MODEL repository of annotated three-dimensional protein structure homology models. Nucleic Acids Res. 32 (2004) D230-D234
    • (2004) Nucleic Acids Res. , vol.32
    • Kopp, J.1    Schwede, T.2
  • 27
    • 0042622380 scopus 로고    scopus 로고
    • The SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. The SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31 (2003) 3381-3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 29
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R., MacArthur M., Moss D., and Thornton J. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 32
    • 0036138028 scopus 로고    scopus 로고
    • Evaluation of a fast implicit solvent model for molecular dynamics simulations
    • Ferrara P., Apostolakis J., and Caflisch A. Evaluation of a fast implicit solvent model for molecular dynamics simulations. Proteins 46 (2002) 24-33
    • (2002) Proteins , vol.46 , pp. 24-33
    • Ferrara, P.1    Apostolakis, J.2    Caflisch, A.3
  • 33
    • 16344362822 scopus 로고    scopus 로고
    • TMDET: web server for detecting transmembrane regions of proteins by using their 3D coordinates
    • Tusnády G.E., Dosztányi Z., and Simon I. TMDET: web server for detecting transmembrane regions of proteins by using their 3D coordinates. Bioinformatics 21 (2005) 1276-1277
    • (2005) Bioinformatics , vol.21 , pp. 1276-1277
    • Tusnády, G.E.1    Dosztányi, Z.2    Simon, I.3
  • 35
    • 0030310393 scopus 로고    scopus 로고
    • Recognition of chiral conformations of the achiral neurotransmitter, γ-aminobutyric acid
    • Simonyi M. Recognition of chiral conformations of the achiral neurotransmitter, γ-aminobutyric acid. Enantiomer 1 (1996) 403-414
    • (1996) Enantiomer , vol.1 , pp. 403-414
    • Simonyi, M.1
  • 36
    • 0012556732 scopus 로고
    • Hydration of cations: H-bond shortening as an electrostatic effect
    • Mayer I., Lukovits I., and Radnai T. Hydration of cations: H-bond shortening as an electrostatic effect. Chem. Phys. Lett. 188 (1992) 595-598
    • (1992) Chem. Phys. Lett. , vol.188 , pp. 595-598
    • Mayer, I.1    Lukovits, I.2    Radnai, T.3
  • 37
    • 27744574834 scopus 로고    scopus 로고
    • Novel parent structures for inhibitors of the murine GABA transporters mGAT3 and mGAT4
    • Kragler A., Höfner G., and Wanner K.T. Novel parent structures for inhibitors of the murine GABA transporters mGAT3 and mGAT4. Eur. J. Pharmacol. 519 (2005) 43-47
    • (2005) Eur. J. Pharmacol. , vol.519 , pp. 43-47
    • Kragler, A.1    Höfner, G.2    Wanner, K.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.