메뉴 건너뛰기




Volumn 387, Issue 1, 2009, Pages 175-191

Pentameric Assembly of Potassium Channel Tetramerization Domain-Containing Protein 5

Author keywords

BTB; GRASP55; KCTD5; Kv channel; T1 domain

Indexed keywords

AMINO ACID; POTASSIUM CHANNEL; POTASSIUM CHANNEL KV1.2; SHAL POTASSIUM CHANNEL; SHAW POTASSIUM CHANNEL; TETRAMERIZATION DOMAIN CONTAINING PROTEIN 5; UNCLASSIFIED DRUG;

EID: 61349202109     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.01.030     Document Type: Article
Times cited : (65)

References (44)
  • 3
    • 0028040875 scopus 로고
    • The POZ domain: a conserved protein-protein interaction motif
    • Bardwell V.J., and Treisman R. The POZ domain: a conserved protein-protein interaction motif. Genes Dev. 8 (1994) 1664-1677
    • (1994) Genes Dev. , vol.8 , pp. 1664-1677
    • Bardwell, V.J.1    Treisman, R.2
  • 4
    • 0028110129 scopus 로고
    • The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila
    • Zollman S., Godt D., Prive G.G., Couderc J., and Laski F.A. The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila. Proc. Natl Acad. Sci. 91 (1994) 10717-10721
    • (1994) Proc. Natl Acad. Sci. , vol.91 , pp. 10717-10721
    • Zollman, S.1    Godt, D.2    Prive, G.G.3    Couderc, J.4    Laski, F.A.5
  • 6
    • 0032304724 scopus 로고    scopus 로고
    • A superfamily of small potassium channel subunits: form and function of the MinK-related peptides (MiRPs)
    • Abbott G.W., and Goldstein S.A.N. A superfamily of small potassium channel subunits: form and function of the MinK-related peptides (MiRPs). Q. Rev. Biophys. 31 (1998) 357-398
    • (1998) Q. Rev. Biophys. , vol.31 , pp. 357-398
    • Abbott, G.W.1    Goldstein, S.A.N.2
  • 8
    • 27744439030 scopus 로고    scopus 로고
    • Directional asymmetry of the zebrafish epithalamus guides dorsoventral innervation of the midbrain target
    • Gamse J.T., Kuan Y.-S., Macurak M., Brosamle C., Thisse B., Thisse C., et al. Directional asymmetry of the zebrafish epithalamus guides dorsoventral innervation of the midbrain target. Development 132 (2005) 4869-4881
    • (2005) Development , vol.132 , pp. 4869-4881
    • Gamse, J.T.1    Kuan, Y.-S.2    Macurak, M.3    Brosamle, C.4    Thisse, B.5    Thisse, C.6
  • 13
    • 33644617753 scopus 로고    scopus 로고
    • Analysis of the human protein interactome and comparison with yeast, worm and fly interaction datasets
    • Gandhi T.K., Zhong J., Mathivanan S., Karthick L., Chandrika K.N., Mohan S.S., et al. Analysis of the human protein interactome and comparison with yeast, worm and fly interaction datasets. Nat. Genet. 38 (2006) 285-293
    • (2006) Nat. Genet. , vol.38 , pp. 285-293
    • Gandhi, T.K.1    Zhong, J.2    Mathivanan, S.3    Karthick, L.4    Chandrika, K.N.5    Mohan, S.S.6
  • 14
    • 49549094267 scopus 로고    scopus 로고
    • Structural specificity in coiled-coil interactions
    • Grigoryan G., and Keating A.E. Structural specificity in coiled-coil interactions. Curr. Opin. Struct. Biol. 18 (2008) 477-483
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 477-483
    • Grigoryan, G.1    Keating, A.E.2
  • 16
    • 0029918694 scopus 로고    scopus 로고
    • The FSSP database: fold classification based on structure-structure alignment of proteins
    • Holm L., and Sander C. The FSSP database: fold classification based on structure-structure alignment of proteins. Nucleic Acids Res. 24 (1996) 206-209
    • (1996) Nucleic Acids Res. , vol.24 , pp. 206-209
    • Holm, L.1    Sander, C.2
  • 17
    • 0001913048 scopus 로고    scopus 로고
    • Predicting protein disorder for N-, C-, and internal regions
    • Li X., Romero P., Rani M., Dunker A.K., and Obradovic Z. Predicting protein disorder for N-, C-, and internal regions. Genome Inf. 10 (1999) 30-40
    • (1999) Genome Inf. , vol.10 , pp. 30-40
    • Li, X.1    Romero, P.2    Rani, M.3    Dunker, A.K.4    Obradovic, Z.5
  • 18
    • 0032724185 scopus 로고    scopus 로고
    • Structure-function studies of the BTB/POZ transcriptional repression domain from the promyelocytic leukemia zinc finger oncoprotein
    • Li X., Peng H., Schultz D.C., Lopez-Guisa J.M., Rauscher III F.J., and Marmorstein R. Structure-function studies of the BTB/POZ transcriptional repression domain from the promyelocytic leukemia zinc finger oncoprotein. Cancer Res. 59 (1999) 5275-5282
    • (1999) Cancer Res. , vol.59 , pp. 5275-5282
    • Li, X.1    Peng, H.2    Schultz, D.C.3    Lopez-Guisa, J.M.4    Rauscher III, F.J.5    Marmorstein, R.6
  • 20
    • 0041806652 scopus 로고    scopus 로고
    • Determining the basis of channel-tetramerization specificity by X-ray crystallography and a sequence-comparison algorithm: family values (FamVal)
    • Nanao M.H., Zhou W., Pfaffinger P.J., and Choe S. Determining the basis of channel-tetramerization specificity by X-ray crystallography and a sequence-comparison algorithm: family values (FamVal). Proc. Natl Acad. Sci. 100 (2003) 8670-8675
    • (2003) Proc. Natl Acad. Sci. , vol.100 , pp. 8670-8675
    • Nanao, M.H.1    Zhou, W.2    Pfaffinger, P.J.3    Choe, S.4
  • 21
    • 0030662715 scopus 로고    scopus 로고
    • GRASP65, a protein involved in the stacking of Golgi cisternae
    • Barr F.A., Puype M., Vandekerckhove J., and Warren G. GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 91 (1997) 253-262
    • (1997) Cell , vol.91 , pp. 253-262
    • Barr, F.A.1    Puype, M.2    Vandekerckhove, J.3    Warren, G.4
  • 22
    • 0033568489 scopus 로고    scopus 로고
    • GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system
    • Shorter J., Watson R., Giannakou M.E., Clarke M., Warren G., and Barr F.A. GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J. 18 (1999) 4949-4960
    • (1999) EMBO J. , vol.18 , pp. 4949-4960
    • Shorter, J.1    Watson, R.2    Giannakou, M.E.3    Clarke, M.4    Warren, G.5    Barr, F.A.6
  • 24
    • 1342333779 scopus 로고    scopus 로고
    • Three-dimensional structure of I(to); Kv4.2-KChIP2 ion channels by electron microscopy at 21 angstrom resolution
    • Kim L.A., Furst J., Gutierrez D., Butler M.H., Xu S., Goldstein S.A., et al. Three-dimensional structure of I(to); Kv4.2-KChIP2 ion channels by electron microscopy at 21 angstrom resolution. Neuron 41 (2004) 513-519
    • (2004) Neuron , vol.41 , pp. 513-519
    • Kim, L.A.1    Furst, J.2    Gutierrez, D.3    Butler, M.H.4    Xu, S.5    Goldstein, S.A.6
  • 26
    • 34250721751 scopus 로고    scopus 로고
    • Exploring and designing protein function with restricted diversity
    • Sidhu S.S., and Kossiakoff A.A. Exploring and designing protein function with restricted diversity. Curr. Opin. Chem. Biol. 11 (2007) 347-354
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 347-354
    • Sidhu, S.S.1    Kossiakoff, A.A.2
  • 27
    • 34247243597 scopus 로고    scopus 로고
    • Identification of a cytoplasmic interaction partner of the large regulatory proteins Rep78/Rep68 of adeno-associated virus type 2 (AAV-2)
    • Weger S., Hammer E., Götz A., and Heilbronn R. Identification of a cytoplasmic interaction partner of the large regulatory proteins Rep78/Rep68 of adeno-associated virus type 2 (AAV-2). Virology 362 (2007) 192-206
    • (2007) Virology , vol.362 , pp. 192-206
    • Weger, S.1    Hammer, E.2    Götz, A.3    Heilbronn, R.4
  • 28
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., and Clardy J. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229 (1993) 105-204
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-204
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0033896691 scopus 로고    scopus 로고
    • Maximum likelihood density modification
    • Terwilliger T.C. Maximum likelihood density modification. Acta Crystallogr. Sect. D 56 (2000) 965-972
    • (2000) Acta Crystallogr. Sect. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 34
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances crystallographic simulated annealing and refinement
    • Adams P.D., Pannu N.S., Read R.J., and Brunger A.T. Cross-validated maximum likelihood enhances crystallographic simulated annealing and refinement. Proc. Natl Acad. Sci. USA 94 (1997) 5018-5023
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5018-5023
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brunger, A.T.4
  • 35
    • 0000560808 scopus 로고    scopus 로고
    • An automated program for molecular replacement: MOLREP
    • Vagin A.A., and Teplyakov A. An automated program for molecular replacement: MOLREP. J. Appl. Crystallogr. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.A.1    Teplyakov, A.2
  • 36
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E. Refinement of macromolecular structures by maximum-likelihood method. Acta Crystallogr. Sect. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.3
  • 38
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: a program for the analysis of the pore dimensions of ion channel structural models
    • Smart O.S., Neduvelil J.G., Wang X., Wallace B.A., and Sansom M.S. HOLE: a program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graphics 14 (1996) 354-360
    • (1996) J. Mol. Graphics , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.5
  • 40
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11 (1991) 281-296
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 41
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The European Molecular Biology Open Software Suite
    • Rice P., Longden I., and Bleasby A. EMBOSS: The European Molecular Biology Open Software Suite. Trends Genet. 16 (2000) 276-277
    • (2000) Trends Genet. , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 42
    • 47249161258 scopus 로고    scopus 로고
    • SA channel complexes include four subunits each of DPP6 and Kv4.2
    • SA channel complexes include four subunits each of DPP6 and Kv4.2. J. Biol. Chem. 283 (2008) 15072-15077
    • (2008) J. Biol. Chem. , vol.283 , pp. 15072-15077
    • Soh, H.1    Goldstein, S.A.N.2
  • 43
    • 0032701484 scopus 로고    scopus 로고
    • Improving biosensor analysis
    • Myszka D.G. Improving biosensor analysis. J. Mol. Recognit. 12 (1999) 279-284
    • (1999) J. Mol. Recognit. , vol.12 , pp. 279-284
    • Myszka, D.G.1
  • 44
    • 0033635789 scopus 로고    scopus 로고
    • + channel currents
    • + channel currents. Eur. Biophys. J. 29 (2000) 555-557
    • (2000) Eur. Biophys. J. , vol.29 , pp. 555-557
    • Clay, J.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.