메뉴 건너뛰기




Volumn 16, Issue 6, 2009, Pages 631-638

The N-terminal domain of GluR6-subtype glutamate receptor ion channels

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR; BINDING PROTEIN; DIMER; G PROTEIN COUPLED RECEPTOR; GLUTAMATE RECEPTOR; GLUTAMATE RECEPTOR 6; GLUTAMATE RECEPTOR ION CHANNEL; ION CHANNEL; ISOLEUCINE VALINE BINDING PROTEIN; KAINIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 67349285101     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1613     Document Type: Article
Times cited : (95)

References (48)
  • 3
    • 0038662595 scopus 로고    scopus 로고
    • Evolution, structure, and activation mechanism of family 3/C G-protein-coupled receptors
    • Pin, J.P., Galvez, T. & Prezeau, L. Evolution, structure, and activation mechanism of family 3/C G-protein-coupled receptors. Pharmacol. Ther. 98, 325-354 (2003).
    • (2003) Pharmacol. Ther , vol.98 , pp. 325-354
    • Pin, J.P.1    Galvez, T.2    Prezeau, L.3
  • 4
    • 0025221685 scopus 로고
    • A family of glutamate receptor genes: Evidence for the formation of heteromultimeric receptors with distinct channel properties
    • Nakanishi, N., Shneider, N.A. & Axel, R. A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties. Neuron 5, 569-581 (1990).
    • (1990) Neuron , vol.5 , pp. 569-581
    • Nakanishi, N.1    Shneider, N.A.2    Axel, R.3
  • 5
    • 0028559605 scopus 로고
    • Agonist-selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid binding proteins
    • Stern-Bach, Y. et al. Agonist-selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid binding proteins. Neuron 13, 1345-1357 (1994).
    • (1994) Neuron , vol.13 , pp. 1345-1357
    • Stern-Bach, Y.1
  • 6
    • 0027295942 scopus 로고
    • The ligand-binding domain in metabotropic glutamate receptors is related to bacterial periplasmic binding proteins
    • O'Hara, P.J. et al. The ligand-binding domain in metabotropic glutamate receptors is related to bacterial periplasmic binding proteins. Neuron 11, 41-52 (1993).
    • (1993) Neuron , vol.11 , pp. 41-52
    • O'Hara, P.J.1
  • 7
    • 0034718925 scopus 로고    scopus 로고
    • Structural basis of glutamate recognition by a dimeric metabo-tropic glutamate receptor
    • Kunishima, N. et al. Structural basis of glutamate recognition by a dimeric metabo-tropic glutamate receptor. Nature 407, 971-977 (2000).
    • (2000) Nature , vol.407 , pp. 971-977
    • Kunishima, N.1
  • 8
    • 0032578635 scopus 로고    scopus 로고
    • Structure of a glutamate-receptor ligand-binding core in complex with kainate
    • Armstrong, N., Sun, Y., Chen, G.Q. & Gouaux, E. Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature 395, 913-917 (1998).
    • (1998) Nature , vol.395 , pp. 913-917
    • Armstrong, N.1    Sun, Y.2    Chen, G.Q.3    Gouaux, E.4
  • 9
    • 0033051714 scopus 로고    scopus 로고
    • A regulatory domain (R1-R2) in the amino terminus of the N-methyl-D-aspartate receptor: Effects of spermine, protons, and ifenprodil, and structural similarity to bacterial leucine/isoleucine/valine binding protein
    • Masuko, T. et al. A regulatory domain (R1-R2) in the amino terminus of the N-methyl-D-aspartate receptor: effects of spermine, protons, and ifenprodil, and structural similarity to bacterial leucine/isoleucine/valine binding protein. Mol. Pharmacol. 55, 957-969 (1999).
    • (1999) Mol. Pharmacol , vol.55 , pp. 957-969
    • Masuko, T.1
  • 10
    • 0034517709 scopus 로고    scopus 로고
    • Molecular organization of a zinc binding N-terminal modulatory domain in a NMDA receptor subunit
    • Paoletti, P. et al. Molecular organization of a zinc binding N-terminal modulatory domain in a NMDA receptor subunit. Neuron 28, 911-925 (2000).
    • (2000) Neuron , vol.28 , pp. 911-925
    • Paoletti, P.1
  • 11
    • 49649122326 scopus 로고    scopus 로고
    • Homology modeling of NR2B modulatory domain of NMDA receptor and analysis of ifenprodil binding
    • Marinelli, L. et al. Homology modeling of NR2B modulatory domain of NMDA receptor and analysis of ifenprodil binding. Chem. Med. Chem. 2, 1498-1510 (2007).
    • (2007) Chem. Med. Chem , vol.2 , pp. 1498-1510
    • Marinelli, L.1
  • 12
    • 58849138886 scopus 로고    scopus 로고
    • Structural basis of NR2B-selective antagonist recognition by NMDA receptors
    • Mony, L. et al. Structural basis of NR2B-selective antagonist recognition by NMDA receptors. Mol. Pharmacol. 75, 60-74 (2009).
    • (2009) Mol. Pharmacol , vol.75 , pp. 60-74
    • Mony, L.1
  • 13
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N- acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves, P.J., Callewaert, N., Contreras, R. & Khorana, H.G. Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N- acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl. Acad. Sci. USA 99, 13419-13424 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 14
    • 0032878510 scopus 로고    scopus 로고
    • Oligomerization and ligand-binding properties of the ectodomain of the α-amino-3-hydroxy- 5-methyl-4-isoxazole propionic acid receptor subunit GluRD
    • Kuusinen, A., Abele, R., Madden, D.R. & Keinanen, K. Oligomerization and ligand-binding properties of the ectodomain of the α-amino-3-hydroxy- 5-methyl-4-isoxazole propionic acid receptor subunit GluRD. J. Biol. Chem. 274, 28937-28943 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 28937-28943
    • Kuusinen, A.1    Abele, R.2    Madden, D.R.3    Keinanen, K.4
  • 15
    • 0035793597 scopus 로고    scopus 로고
    • Assembly and ligand binding properties of the water-soluble extracellular domains of the glutamate receptor 1 subunit
    • Wells, G.B., Lin, L., Jeanclos, E.M. & Anand, R. Assembly and ligand binding properties of the water-soluble extracellular domains of the glutamate receptor 1 subunit. J. Biol. Chem. 276, 3031-3036 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 3031-3036
    • Wells, G.B.1    Lin, L.2    Jeanclos, E.M.3    Anand, R.4
  • 16
    • 67649565613 scopus 로고    scopus 로고
    • Crystal structure and association behavior of the GluR2 amino terminal domain
    • in the press
    • Jin, R. et al. Crystal structure and association behavior of the GluR2 amino terminal domain. EMBO J. (in the press).
    • EMBO J
    • Jin, R.1
  • 17
    • 0042011224 scopus 로고    scopus 로고
    • Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals
    • Kantardjieff, K.A. & Rupp, B. Matthews coefficient probabilities: improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals. Protein Sci. 12, 1865-1871 (2003).
    • (2003) Protein Sci , vol.12 , pp. 1865-1871
    • Kantardjieff, K.A.1    Rupp, B.2
  • 18
    • 13844266202 scopus 로고    scopus 로고
    • Crystal Structures of the GluR5 and GluR6 ligand binding cores: Molecular mechanisms underlying kainate receptor selectivity
    • Mayer, M.L. Crystal Structures of the GluR5 and GluR6 ligand binding cores: molecular mechanisms underlying kainate receptor selectivity. Neuron 45, 539-552 (2005).
    • (2005) Neuron , vol.45 , pp. 539-552
    • Mayer, M.L.1
  • 20
    • 34247210665 scopus 로고    scopus 로고
    • Structures of the extracellular regions of the group II/III metabotropic glutamate receptors
    • Muto, T., Tsuchiya, D., Morikawa, K. & Jingami, H. Structures of the extracellular regions of the group II/III metabotropic glutamate receptors. Proc. Natl. Acad. Sci. USA 104, 3759-3764 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 3759-3764
    • Muto, T.1    Tsuchiya, D.2    Morikawa, K.3    Jingami, H.4
  • 21
    • 2442488034 scopus 로고    scopus 로고
    • Appropriate NR1-NR1 disulfide-linked homodimer formation is requisite for efficient expression of functional, cell surface N-methyl-D-aspartate NR1/NR2 receptors
    • Papadakis, M., Hawkins, L.M. & Stephenson, F.A. Appropriate NR1-NR1 disulfide-linked homodimer formation is requisite for efficient expression of functional, cell surface N-methyl-D-aspartate NR1/NR2 receptors. J. Biol. Chem. 279, 14703-14712 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 14703-14712
    • Papadakis, M.1    Hawkins, L.M.2    Stephenson, F.A.3
  • 23
    • 0000484499 scopus 로고
    • Hydrophobic paramete π of amino acid side chains from partitioning of N-acetyl-amino amides
    • Fauchere, J.L. & Pliska, V. Hydrophobic paramete π of amino acid side chains from partitioning of N-acetyl-amino amides. Eur. J. Med. Chem. 18, 369-375 (1983).
    • (1983) Eur. J. Med. Chem , vol.18 , pp. 369-375
    • Fauchere, J.L.1    Pliska, V.2
  • 24
    • 0025259963 scopus 로고
    • Cloning of a novel glutamate receptor subunit, GluR5: Expression in the nervous system during development
    • Bettler, B. et al. Cloning of a novel glutamate receptor subunit, GluR5: expression in the nervous system during development. Neuron 5, 583-595 (1990).
    • (1990) Neuron , vol.5 , pp. 583-595
    • Bettler, B.1
  • 25
    • 13444302564 scopus 로고    scopus 로고
    • Structure and different conformational states of native AMPA receptor complexes
    • Nakagawa, T., Cheng, Y., Ramm, E., Sheng, M. & Walz, T. Structure and different conformational states of native AMPA receptor complexes. Nature 433, 545-549 (2005).
    • (2005) Nature , vol.433 , pp. 545-549
    • Nakagawa, T.1    Cheng, Y.2    Ramm, E.3    Sheng, M.4    Walz, T.5
  • 26
    • 7444240214 scopus 로고    scopus 로고
    • The three-dimensional structure of an ionotropic glutamate receptor reveals a dimer-of-dimers assembly
    • Tichelaar, W., Safferling, M., Keinanen, K., Stark, H. & Madden, D.R. The three-dimensional structure of an ionotropic glutamate receptor reveals a dimer-of-dimers assembly. J. Mol. Biol. 344, 435-442 (2004).
    • (2004) J. Mol. Biol , vol.344 , pp. 435-442
    • Tichelaar, W.1    Safferling, M.2    Keinanen, K.3    Stark, H.4    Madden, D.R.5
  • 27
    • 50149084710 scopus 로고    scopus 로고
    • The quaternary structure of a calcium-permeable AMPA receptor: Conservation of shape and symmetry across functionally distinct subunit assemblies
    • Midgett, C.R. & Madden, D.R. The quaternary structure of a calcium-permeable AMPA receptor: conservation of shape and symmetry across functionally distinct subunit assemblies. J. Mol. Biol. 382, 578-584 (2008).
    • (2008) J. Mol. Biol , vol.382 , pp. 578-584
    • Midgett, C.R.1    Madden, D.R.2
  • 28
    • 20344362178 scopus 로고    scopus 로고
    • Amino acid recognition by venus flytrap domains is encoded in an 8-residue motif
    • Acher, F.C. & Bertrand, H.O. Amino acid recognition by venus flytrap domains is encoded in an 8-residue motif. Biopolymers 80, 357-366 (2005).
    • (2005) Biopolymers , vol.80 , pp. 357-366
    • Acher, F.C.1    Bertrand, H.O.2
  • 29
    • 0036759170 scopus 로고    scopus 로고
    • B receptor is required for activation and allosteric interaction between the subunits
    • B receptor is required for activation and allosteric interaction between the subunits. J. Neurosci. 22, 7352-7361 (2002).
    • (2002) J. Neurosci , vol.22 , pp. 7352-7361
    • Kniazeff, J.1    Galvez, T.2    Labesse, G.3    Pin, J.P.4
  • 30
    • 43249098905 scopus 로고    scopus 로고
    • B receptor extracellular domain revealed by glycan wedge scanning
    • B receptor extracellular domain revealed by glycan wedge scanning. EMBO J. 27, 1321-1332 (2008).
    • (2008) EMBO J , vol.27 , pp. 1321-1332
    • Rondard, P.1
  • 31
    • 37549045649 scopus 로고    scopus 로고
    • Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition
    • Gielen, M. et al. Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition. Neuron 57, 80-93 (2008).
    • (2008) Neuron , vol.57 , pp. 80-93
    • Gielen, M.1
  • 32
    • 33745912405 scopus 로고    scopus 로고
    • A time- and cost-efficient system for high-level protein production in mammalian cells
    • Aricescu, A.R., Lu, W. & Jones, E.Y. A time- and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallogr. D Biol. Crystallogr. 62, 1243-1250 (2006).
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 277, 307-326 (1997).
    • (1997) Methods Enzymol , vol.277 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A.J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 35
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams, P.D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D Biol. Crystallogr. 58, 1948-1954 (2002).
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 36
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J. & Merritt, E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 62, 439-450 (2006).
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 37
  • 38
    • 3242886389 scopus 로고    scopus 로고
    • MOLPROBITY: Structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis, I.W., Murray, L.W., Richardson, J.S. & Richardson, D.C. MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Res. 32, W615-W619 (2004).
    • (2004) Nucleic Acids Res , vol.32
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 39
    • 0028103275 scopus 로고
    • Number 4. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr , vol.50 , pp. 760-763
  • 41
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 42
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: The projection of evolutionary conservation scores of residues on protein structures
    • Landau, M. et al. ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res. 33, W299-W302 (2005).
    • (2005) Nucleic Acids Res , vol.33
    • Landau, M.1
  • 43
    • 57549085173 scopus 로고    scopus 로고
    • Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation
    • Unit 18.15
    • Brown, P.H., Balbo, A. & Schuck, P. Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation. Curr. Protoc. Immunol. Chapter 18, Unit 18.15 (2008).
    • (2008) Curr. Protoc. Immunol. Chapter , vol.18
    • Brown, P.H.1    Balbo, A.2    Schuck, P.3
  • 44
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck, P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 78, 1606-1619 (2000).
    • (2000) Biophys. J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 45
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • Schuck, P. On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation. Anal. Biochem. 320, 104-124 (2003).
    • (2003) Anal. Biochem , vol.320 , pp. 104-124
    • Schuck, P.1
  • 46
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • García De La Torre, J., Huertas, M.L. & Carrasco, B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78, 719-730 (2000).
    • (2000) Biophys. J , vol.78 , pp. 719-730
    • García De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 48
    • 1442274756 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition
    • Vistica, J. et al. Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition. Anal. Biochem. 326, 234-256 (2004).
    • (2004) Anal. Biochem , vol.326 , pp. 234-256
    • Vistica, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.