메뉴 건너뛰기




Volumn 425, Issue 14, 2013, Pages 2509-2528

Ligand-induced dynamic changes in extended PDZ domains from NHERF1

Author keywords

ligand binding; NMR; PDZ domain; protein structure; scaffolding proteins

Indexed keywords

HELIX LOOP HELIX PROTEIN; PROTEIN NHERF1; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84879556288     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.04.001     Document Type: Article
Times cited : (26)

References (93)
  • 1
    • 0034740693 scopus 로고    scopus 로고
    • Mechanisms and role of PDZ domains in signalling complex assembly
    • B.Z. Harris, and W.A. Lim Mechanisms and role of PDZ domains in signalling complex assembly J. Cell Sci. 114 2001 3219 3231
    • (2001) J. Cell Sci. , vol.114 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 2
    • 36248996466 scopus 로고    scopus 로고
    • Scaffold proteins as dynamic switches
    • M. Zhang Scaffold proteins as dynamic switches Nat. Chem. Biol. 3 2007 756 757
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 756-757
    • Zhang, M.1
  • 3
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • D.A. Doyle, A. Lee, J. Lewis, E. Kim, M. Sheng, and R. MacKinnon Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ Cell 85 1996 1067 1076
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    Mackinnon, R.6
  • 4
    • 0034721943 scopus 로고    scopus 로고
    • Formation of nNOS/PSD-95 PDZ dimer requires a preformed β-finger structure from the nNOS PDZ domain
    • H. Tochio, Y.K. Mok, Q. Zhang, H.M. Kan, D.S. Bredt, and M. Zhang Formation of nNOS/PSD-95 PDZ dimer requires a preformed β-finger structure from the nNOS PDZ domain J. Mol. Biol. 303 2000 359 370
    • (2000) J. Mol. Biol. , vol.303 , pp. 359-370
    • Tochio, H.1    Mok, Y.K.2    Zhang, Q.3    Kan, H.M.4    Bredt, D.S.5    Zhang, M.6
  • 6
    • 33646009701 scopus 로고    scopus 로고
    • The association of NHERF adaptor proteins with G protein-coupled receptors and receptor tyrosine kinases
    • E.J. Weinman, R.A. Hall, P.A. Friedman, L.Y. Liu-Chen, and S. Shenolikar The association of NHERF adaptor proteins with G protein-coupled receptors and receptor tyrosine kinases Annu. Rev. Physiol. 68 2006 491 505
    • (2006) Annu. Rev. Physiol. , vol.68 , pp. 491-505
    • Weinman, E.J.1    Hall, R.A.2    Friedman, P.A.3    Liu-Chen, L.Y.4    Shenolikar, S.5
  • 7
  • 9
    • 77951763488 scopus 로고    scopus 로고
    • A regulated complex of the scaffolding proteins PDZK1 and EBP50 with ezrin contribute to microvillar organization
    • D.P. LaLonde, D. Garbett, and A. Bretscher A regulated complex of the scaffolding proteins PDZK1 and EBP50 with ezrin contribute to microvillar organization Mol. Biol. Cell 21 2010 1519 1529
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1519-1529
    • Lalonde, D.P.1    Garbett, D.2    Bretscher, A.3
  • 10
    • 0030608877 scopus 로고    scopus 로고
    • Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family
    • D. Reczek, M. Berryman, and A. Bretscher Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family J. Cell Biol. 139 1997 169 179
    • (1997) J. Cell Biol. , vol.139 , pp. 169-179
    • Reczek, D.1    Berryman, M.2    Bretscher, A.3
  • 12
    • 27844570909 scopus 로고    scopus 로고
    • + exchanger regulatory factor and the cystic fibrosis transmembrane conductance regulator
    • + exchanger regulatory factor and the cystic fibrosis transmembrane conductance regulator J. Biol. Chem. 280 2005 37634 37643
    • (2005) J. Biol. Chem. , vol.280 , pp. 37634-37643
    • Li, J.1    Dai, Z.2    Jana, D.3    Callaway, D.J.4    Bu, Z.5
  • 13
    • 34147206059 scopus 로고    scopus 로고
    • NHERF1/EBP50 head-to-tail intramolecular interaction masks association with PDZ domain ligands
    • F.C. Morales, Y. Takahashi, S. Momin, H. Adams, X. Chen, and M.M. Georgescu NHERF1/EBP50 head-to-tail intramolecular interaction masks association with PDZ domain ligands Mol. Cell. Biol. 27 2007 2527 2537
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 2527-2537
    • Morales, F.C.1    Takahashi, Y.2    Momin, S.3    Adams, H.4    Chen, X.5    Georgescu, M.M.6
  • 14
    • 68949167656 scopus 로고    scopus 로고
    • Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1
    • J. Li, D.J. Callaway, and Z. Bu Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1 J. Mol. Biol. 392 2009 166 180
    • (2009) J. Mol. Biol. , vol.392 , pp. 166-180
    • Li, J.1    Callaway, D.J.2    Bu, Z.3
  • 15
    • 77951212822 scopus 로고    scopus 로고
    • A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation
    • S. Bhattacharya, Z. Dai, J. Li, S. Baxter, D.J. Callaway, D. Cowburn, and Z. Bu A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation J. Biol. Chem. 285 2010 9981 9994
    • (2010) J. Biol. Chem. , vol.285 , pp. 9981-9994
    • Bhattacharya, S.1    Dai, Z.2    Li, J.3    Baxter, S.4    Callaway, D.J.5    Cowburn, D.6    Bu, Z.7
  • 16
    • 34848850791 scopus 로고    scopus 로고
    • + exchanger regulatory factor 1 autoinhibition and promotes cystic fibrosis transmembrane conductance regulator macromolecular assembly
    • + exchanger regulatory factor 1 autoinhibition and promotes cystic fibrosis transmembrane conductance regulator macromolecular assembly J. Biol. Chem. 282 2007 27086 27099
    • (2007) J. Biol. Chem. , vol.282 , pp. 27086-27099
    • Li, J.1    Poulikakos, P.I.2    Dai, Z.3    Testa, J.R.4    Callaway, D.J.5    Bu, Z.6
  • 17
    • 78649251653 scopus 로고    scopus 로고
    • Activation of nanoscale allosteric protein domain motion revealed by neutron spin echo spectroscopy
    • B. Farago, J. Li, G. Cornilescu, D.J. Callaway, and Z. Bu Activation of nanoscale allosteric protein domain motion revealed by neutron spin echo spectroscopy Biophys. J. 99 2010 3473 3482
    • (2010) Biophys. J. , vol.99 , pp. 3473-3482
    • Farago, B.1    Li, J.2    Cornilescu, G.3    Callaway, D.J.4    Bu, Z.5
  • 19
    • 62849105308 scopus 로고    scopus 로고
    • Creating conformational entropy by increasing interdomain mobility in ligand binding regulation: A revisit to N-terminal tandem PDZ domains of PSD-95
    • W. Wang, J. Weng, X. Zhang, M. Liu, and M. Zhang Creating conformational entropy by increasing interdomain mobility in ligand binding regulation: a revisit to N-terminal tandem PDZ domains of PSD-95 J. Am. Chem. Soc. 131 2009 787 796
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 787-796
    • Wang, W.1    Weng, J.2    Zhang, X.3    Liu, M.4    Zhang, M.5
  • 20
    • 84863798401 scopus 로고    scopus 로고
    • Ezrin-anchored protein kinase A coordinates phosphorylation-dependent disassembly of a NHERF1 ternary complex to regulate hormone-sensitive phosphate transport
    • B. Wang, C.K. Means, Y. Yang, T. Mamonova, A. Bisello, and D.L. Altschuler Ezrin-anchored protein kinase A coordinates phosphorylation-dependent disassembly of a NHERF1 ternary complex to regulate hormone-sensitive phosphate transport J. Biol. Chem. 287 2012 24148 24163
    • (2012) J. Biol. Chem. , vol.287 , pp. 24148-24163
    • Wang, B.1    Means, C.K.2    Yang, Y.3    Mamonova, T.4    Bisello, A.5    Altschuler, D.L.6
  • 21
    • 0032541057 scopus 로고    scopus 로고
    • The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule
    • D. Reczek, and A. Bretscher The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule J. Biol. Chem. 273 1998 18452 18458
    • (1998) J. Biol. Chem. , vol.273 , pp. 18452-18458
    • Reczek, D.1    Bretscher, A.2
  • 23
    • 0032080043 scopus 로고    scopus 로고
    • Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR)
    • S. Wang, R.W. Raab, P.J. Schatz, W.B. Guggino, and M. Li Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR) FEBS Lett. 427 1998 103 108
    • (1998) FEBS Lett. , vol.427 , pp. 103-108
    • Wang, S.1    Raab, R.W.2    Schatz, P.J.3    Guggino, W.B.4    Li, M.5
  • 24
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA
    • J.R. Riordan, J.M. Rommens, B. Kerem, N. Alon, R. Rozmahel, and Z. Grzelczak Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA Science 245 1989 1066 1073
    • (1989) Science , vol.245 , pp. 1066-1073
    • Riordan, J.R.1    Rommens, J.M.2    Kerem, B.3    Alon, N.4    Rozmahel, R.5    Grzelczak, Z.6
  • 25
    • 80052330284 scopus 로고    scopus 로고
    • Analysis of CFTR interactome in the macromolecular complexes
    • C. Li, and A.P. Naren Analysis of CFTR interactome in the macromolecular complexes Methods Mol. Biol. 741 2011 255 270
    • (2011) Methods Mol. Biol. , vol.741 , pp. 255-270
    • Li, C.1    Naren, A.P.2
  • 26
    • 0035970113 scopus 로고    scopus 로고
    • Regulation of cystic fibrosis transmembrane conductance regulator single-channel gating by bivalent PDZ-domain-mediated interaction
    • V. Raghuram, D.O. Mak, and J.K. Foskett Regulation of cystic fibrosis transmembrane conductance regulator single-channel gating by bivalent PDZ-domain-mediated interaction Proc. Natl Acad. Sci. USA 98 2001 1300 1305
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 1300-1305
    • Raghuram, V.1    Mak, D.O.2    Foskett, J.K.3
  • 27
    • 0037131297 scopus 로고    scopus 로고
    • PDZ domain interaction controls the endocytic recycling of the cystic fibrosis transmembrane conductance regulator
    • A. Swiatecka-Urban, M. Duhaime, B. Coutermarsh, K.H. Karlson, J. Collawn, and M. Milewski PDZ domain interaction controls the endocytic recycling of the cystic fibrosis transmembrane conductance regulator J. Biol. Chem. 277 2002 40099 40105
    • (2002) J. Biol. Chem. , vol.277 , pp. 40099-40105
    • Swiatecka-Urban, A.1    Duhaime, M.2    Coutermarsh, B.3    Karlson, K.H.4    Collawn, J.5    Milewski, M.6
  • 29
    • 75649086188 scopus 로고    scopus 로고
    • + exchanger regulatory factor 1 overexpression-dependent increase of cytoskeleton organization is fundamental in the rescue of F508del cystic fibrosis transmembrane conductance regulator in human airway CFBE41o - Cells
    • + exchanger regulatory factor 1 overexpression-dependent increase of cytoskeleton organization is fundamental in the rescue of F508del cystic fibrosis transmembrane conductance regulator in human airway CFBE41o - cells Mol. Biol. Cell 21 2010 73 86
    • (2010) Mol. Biol. Cell , vol.21 , pp. 73-86
    • Favia, M.1    Guerra, L.2    Fanelli, T.3    Cardone, R.A.4    Monterisi, S.5    Di Sole, F.6
  • 31
    • 0035906714 scopus 로고    scopus 로고
    • Crystal structure of the PDZ1 domain of human Na(+)/H(+) exchanger regulatory factor provides insights into the mechanism of carboxyl-terminal leucine recognition by class i PDZ domains
    • S. Karthikeyan, T. Leung, G. Birrane, G. Webster, and J.A. Ladias Crystal structure of the PDZ1 domain of human Na(+)/H(+) exchanger regulatory factor provides insights into the mechanism of carboxyl-terminal leucine recognition by class I PDZ domains J. Mol. Biol. 308 2001 963 973
    • (2001) J. Mol. Biol. , vol.308 , pp. 963-973
    • Karthikeyan, S.1    Leung, T.2    Birrane, G.3    Webster, G.4    Ladias, J.A.5
  • 32
  • 33
    • 33947712970 scopus 로고    scopus 로고
    • Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions
    • J.M. Elkins, E. Papagrigoriou, G. Berridge, X. Yang, C. Phillips, and C. Gileadi Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions Protein Sci. 16 2007 683 694
    • (2007) Protein Sci. , vol.16 , pp. 683-694
    • Elkins, J.M.1    Papagrigoriou, E.2    Berridge, G.3    Yang, X.4    Phillips, C.5    Gileadi, C.6
  • 35
    • 84859181499 scopus 로고    scopus 로고
    • Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution
    • J. Kim, I. Kim, J.S. Yang, Y.E. Shin, J. Hwang, and S. Park Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution PLoS Genet. 8 2012 e1002510
    • (2012) PLoS Genet. , vol.8 , pp. 1002510
    • Kim, J.1    Kim, I.2    Yang, J.S.3    Shin, Y.E.4    Hwang, J.5    Park, S.6
  • 36
    • 0347753736 scopus 로고    scopus 로고
    • Ligand-dependent dynamics and intramolecular signaling in a PDZ domain
    • E.J. Fuentes, C.J. Der, and A.L. Lee Ligand-dependent dynamics and intramolecular signaling in a PDZ domain J. Mol. Biol. 335 2004 1105 1115
    • (2004) J. Mol. Biol. , vol.335 , pp. 1105-1115
    • Fuentes, E.J.1    Der, C.J.2    Lee, A.L.3
  • 38
    • 0037436384 scopus 로고    scopus 로고
    • Supramodular structure and synergistic target binding of the N-terminal tandem PDZ domains of PSD-95
    • J.F. Long, H. Tochio, P. Wang, J.S. Fan, C. Sala, and M. Niethammer Supramodular structure and synergistic target binding of the N-terminal tandem PDZ domains of PSD-95 J. Mol. Biol. 327 2003 203 214
    • (2003) J. Mol. Biol. , vol.327 , pp. 203-214
    • Long, J.F.1    Tochio, H.2    Wang, P.3    Fan, J.S.4    Sala, C.5    Niethammer, M.6
  • 39
    • 0033617473 scopus 로고    scopus 로고
    • Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex
    • B.J. Hillier, K.S. Christopherson, K.E. Prehoda, D.S. Bredt, and W.A. Lim Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex Science 284 1999 812 815
    • (1999) Science , vol.284 , pp. 812-815
    • Hillier, B.J.1    Christopherson, K.S.2    Prehoda, K.E.3    Bredt, D.S.4    Lim, W.A.5
  • 40
    • 15644379801 scopus 로고    scopus 로고
    • Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
    • Z. Songyang, A.S. Fanning, C. Fu, J. Xu, S.M. Marfatia, and A.H. Chishti Recognition of unique carboxyl-terminal motifs by distinct PDZ domains Science 275 1997 73 76
    • (1997) Science , vol.275 , pp. 73-76
    • Songyang, Z.1    Fanning, A.S.2    Fu, C.3    Xu, J.4    Marfatia, S.M.5    Chishti, A.H.6
  • 41
    • 80055066238 scopus 로고    scopus 로고
    • Change in allosteric network affects binding affinities of PDZ domains: Analysis through perturbation response scanning
    • Z.N. Gerek, and S.B. Ozkan Change in allosteric network affects binding affinities of PDZ domains: analysis through perturbation response scanning PLoS Comput. Biol. 7 2011 e1002154
    • (2011) PLoS Comput. Biol. , vol.7 , pp. 1002154
    • Gerek, Z.N.1    Ozkan, S.B.2
  • 42
    • 84864615365 scopus 로고    scopus 로고
    • Plasticity of PDZ domains in ligand recognition and signaling
    • Y. Ivarsson Plasticity of PDZ domains in ligand recognition and signaling FEBS Lett. 586 2012 2638 2647
    • (2012) FEBS Lett. , vol.586 , pp. 2638-2647
    • Ivarsson, Y.1
  • 43
    • 84861117819 scopus 로고    scopus 로고
    • Beyond the binding site: The role of the βâ-βâ loop and extra-domain structures in PDZ domains
    • S. Mostarda, D. Gfeller, and F. Rao Beyond the binding site: the role of the βâ-βâ loop and extra-domain structures in PDZ domains PLoS Comput. Biol. 8 2012 e1002429
    • (2012) PLoS Comput. Biol. , vol.8 , pp. 1002429
    • Mostarda, S.1    Gfeller, D.2    Rao, F.3
  • 44
    • 52249089383 scopus 로고    scopus 로고
    • The relative binding affinities of PDZ partners for CFTR: A biochemical basis for efficient endocytic recycling
    • P.R. Cushing, A. Fellows, D. Villone, P. Boisguerin, and D.R. Madden The relative binding affinities of PDZ partners for CFTR: a biochemical basis for efficient endocytic recycling Biochemistry 47 2008 10084 10098
    • (2008) Biochemistry , vol.47 , pp. 10084-10098
    • Cushing, P.R.1    Fellows, A.2    Villone, D.3    Boisguerin, P.4    Madden, D.R.5
  • 45
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • C. Chothia, and A.M. Lesk The relation between the divergence of sequence and structure in proteins EMBO J. 5 1986 823 826
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 47
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graphics 14 1996 51 55
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 49
    • 0035827518 scopus 로고    scopus 로고
    • + exchanger regulatory factor PDZ1 interaction with the carboxyl-terminal region of the cystic fibrosis transmembrane conductance regulator
    • + exchanger regulatory factor PDZ1 interaction with the carboxyl-terminal region of the cystic fibrosis transmembrane conductance regulator J. Biol. Chem. 276 2001 19683 19686
    • (2001) J. Biol. Chem. , vol.276 , pp. 19683-19686
    • Karthikeyan, S.1    Leung, T.2    Ladias, J.A.3
  • 50
    • 0034282899 scopus 로고    scopus 로고
    • The PDZ-interacting domain of cystic fibrosis transmembrane conductance regulator is required for functional expression in the apical plasma membrane
    • B.D. Moyer, M. Duhaime, C. Shaw, J. Denton, D. Reynolds, and K.H. Karlson The PDZ-interacting domain of cystic fibrosis transmembrane conductance regulator is required for functional expression in the apical plasma membrane J. Biol. Chem. 275 2000 27069 27074
    • (2000) J. Biol. Chem. , vol.275 , pp. 27069-27074
    • Moyer, B.D.1    Duhaime, M.2    Shaw, C.3    Denton, J.4    Reynolds, D.5    Karlson, K.H.6
  • 51
    • 84859575417 scopus 로고    scopus 로고
    • Structural basis for NHERF1 PDZ domain binding
    • T. Mamonova, M. Kurnikova, and P.A. Friedman Structural basis for NHERF1 PDZ domain binding Biochemistry 51 2012 3110 3120
    • (2012) Biochemistry , vol.51 , pp. 3110-3120
    • Mamonova, T.1    Kurnikova, M.2    Friedman, P.A.3
  • 53
    • 0026784152 scopus 로고
    • Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments
    • J.W. Peng, and G. Wagner Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments Biochemistry 31 1992 8571 8586
    • (1992) Biochemistry , vol.31 , pp. 8571-8586
    • Peng, J.W.1    Wagner, G.2
  • 55
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • A.M. Mandel, M. Akke, and A.G. Palmer III Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme J. Mol. Biol. 246 1995 144 163
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer Iii, A.G.3
  • 56
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy
    • J.P. Loria, M. Rance, and A.G. Palmer A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy J. Am. Chem. Soc. 121 1999 2331 2332
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 58
    • 37349021389 scopus 로고    scopus 로고
    • Interesting structural and dynamical behaviors exhibited by the AF-6 PDZ domain upon Bcr peptide binding
    • X. Niu, Q. Chen, J. Zhang, W. Shen, Y. Shi, and J. Wu Interesting structural and dynamical behaviors exhibited by the AF-6 PDZ domain upon Bcr peptide binding Biochemistry 46 2007 15042 15053
    • (2007) Biochemistry , vol.46 , pp. 15042-15053
    • Niu, X.1    Chen, Q.2    Zhang, J.3    Shen, W.4    Shi, Y.5    Wu, J.6
  • 59
    • 44349160152 scopus 로고    scopus 로고
    • Conformational change upon ligand binding and dynamics of the PDZ domain from leukemia-associated Rho guanine nucleotide exchange factor
    • J. Liu, J. Zhang, Y. Yang, H. Huang, W. Shen, and Q. Hu Conformational change upon ligand binding and dynamics of the PDZ domain from leukemia-associated Rho guanine nucleotide exchange factor Protein Sci. 17 2008 1003 1014
    • (2008) Protein Sci. , vol.17 , pp. 1003-1014
    • Liu, J.1    Zhang, J.2    Yang, Y.3    Huang, H.4    Shen, W.5    Hu, Q.6
  • 60
    • 38449102038 scopus 로고    scopus 로고
    • The multi-PDZ domain protein MUPP1 as a lipid raft-associated scaffolding protein controlling the acrosome reaction in mammalian spermatozoa
    • F. Ackermann, N. Zitranski, D. Heydecke, B. Wilhelm, T. Gudermann, and I. Boekhoff The multi-PDZ domain protein MUPP1 as a lipid raft-associated scaffolding protein controlling the acrosome reaction in mammalian spermatozoa J. Cell. Physiol. 214 2008 757 768
    • (2008) J. Cell. Physiol. , vol.214 , pp. 757-768
    • Ackermann, F.1    Zitranski, N.2    Heydecke, D.3    Wilhelm, B.4    Gudermann, T.5    Boekhoff, I.6
  • 61
    • 58549092371 scopus 로고    scopus 로고
    • Organization and dynamics of PDZ-domain-related supramodules in the postsynaptic density
    • W. Feng, and M. Zhang Organization and dynamics of PDZ-domain-related supramodules in the postsynaptic density Nat. Rev. Neurosci. 10 2009 87 99
    • (2009) Nat. Rev. Neurosci. , vol.10 , pp. 87-99
    • Feng, W.1    Zhang, M.2
  • 62
    • 84864984368 scopus 로고    scopus 로고
    • PDZ interactions regulate rapid turnover of the scaffolding protein EBP50 in microvilli
    • D. Garbett, and A. Bretscher PDZ interactions regulate rapid turnover of the scaffolding protein EBP50 in microvilli J. Cell Biol. 198 2012 195 203
    • (2012) J. Cell Biol. , vol.198 , pp. 195-203
    • Garbett, D.1    Bretscher, A.2
  • 63
    • 77958500001 scopus 로고    scopus 로고
    • The scaffolding protein EBP50 regulates microvillar assembly in a phosphorylation-dependent manner
    • D. Garbett, D.P. LaLonde, and A. Bretscher The scaffolding protein EBP50 regulates microvillar assembly in a phosphorylation-dependent manner J. Cell Biol. 191 2010 397 413
    • (2010) J. Cell Biol. , vol.191 , pp. 397-413
    • Garbett, D.1    Lalonde, D.P.2    Bretscher, A.3
  • 65
    • 79953153131 scopus 로고    scopus 로고
    • Extensions of PDZ domains as important structural and functional elements
    • C.K. Wang, L. Pan, J. Chen, and M. Zhang Extensions of PDZ domains as important structural and functional elements Protein Cell 1 2010 737 751
    • (2010) Protein Cell , vol.1 , pp. 737-751
    • Wang, C.K.1    Pan, L.2    Chen, J.3    Zhang, M.4
  • 66
    • 84868600086 scopus 로고    scopus 로고
    • Interactions outside the boundaries of the canonical binding groove of a PDZ domain influence ligand binding
    • C.N. Chi, S.R. Haq, S. Rinaldo, J. Dogan, F. Cutruzzolà, and Å. Engström Interactions outside the boundaries of the canonical binding groove of a PDZ domain influence ligand binding Biochemistry 51 2012 8971 8979
    • (2012) Biochemistry , vol.51 , pp. 8971-8979
    • Chi, C.N.1    Haq, S.R.2    Rinaldo, S.3    Dogan, J.4    Cutruzzolà, F.5    Engström, Å.6
  • 67
    • 84861194648 scopus 로고    scopus 로고
    • Extensions of PSD-95/discs large/ZO-1 (PDZ) domains influence lipid binding and membrane targeting of syntenin-1
    • A.M. Wawrzyniak, E. Vermeiren, P. Zimmermann, and Y. Ivarsson Extensions of PSD-95/discs large/ZO-1 (PDZ) domains influence lipid binding and membrane targeting of syntenin-1 FEBS Lett. 586 2012 1445 1451
    • (2012) FEBS Lett. , vol.586 , pp. 1445-1451
    • Wawrzyniak, A.M.1    Vermeiren, E.2    Zimmermann, P.3    Ivarsson, Y.4
  • 68
    • 84864590078 scopus 로고    scopus 로고
    • The emerging contribution of sequence context to the specificity of protein interactions mediated by PDZ domains
    • K. Luck, S. Charbonnier, and G. Travé The emerging contribution of sequence context to the specificity of protein interactions mediated by PDZ domains FEBS Lett. 586 2012 2648 2661
    • (2012) FEBS Lett. , vol.586 , pp. 2648-2661
    • Luck, K.1    Charbonnier, S.2    Travé, G.3
  • 69
    • 34248214225 scopus 로고    scopus 로고
    • NMR studies of interactions between C-terminal tail of Kir2.1 channel and PDZ1,2 domains of PSD95
    • S. Pegan, J. Tan, A. Huang, P.A. Slesinger, R. Riek, and S. Choe NMR studies of interactions between C-terminal tail of Kir2.1 channel and PDZ1,2 domains of PSD95 Biochemistry 46 2007 5315 5322
    • (2007) Biochemistry , vol.46 , pp. 5315-5322
    • Pegan, S.1    Tan, J.2    Huang, A.3    Slesinger, P.A.4    Riek, R.5    Choe, S.6
  • 70
    • 79954992086 scopus 로고    scopus 로고
    • Mechanism underlying selective regulation of G protein-gated inwardly rectifying potassium channels by the psychostimulant-sensitive sorting nexin 27
    • B. Balana, I. Maslennikov, W. Kwiatkowski, K.M. Stern, L. Bahima, S. Choe, and P.A. Slesinger Mechanism underlying selective regulation of G protein-gated inwardly rectifying potassium channels by the psychostimulant- sensitive sorting nexin 27 Proc. Natl Acad. Sci. USA 108 2011 5831 5836
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 5831-5836
    • Balana, B.1    Maslennikov, I.2    Kwiatkowski, W.3    Stern, K.M.4    Bahima, L.5    Choe, S.6    Slesinger, P.A.7
  • 71
    • 6344219895 scopus 로고    scopus 로고
    • Is allostery an intrinsic property of all dynamic proteins?
    • K. Gunasekaran, B. Ma, and R. Nussinov Is allostery an intrinsic property of all dynamic proteins? Proteins 57 2004 433 443
    • (2004) Proteins , vol.57 , pp. 433-443
    • Gunasekaran, K.1    Ma, B.2    Nussinov, R.3
  • 72
    • 84864065499 scopus 로고    scopus 로고
    • Protein function and allostery: A dynamic relationship
    • C.G. Kalodimos Protein function and allostery: a dynamic relationship Ann. N. Y. Acad. Sci. 1260 2012 81 86
    • (2012) Ann. N. Y. Acad. Sci. , vol.1260 , pp. 81-86
    • Kalodimos, C.G.1
  • 73
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • S.W. Lockless, and R. Ranganathan Evolutionarily conserved pathways of energetic connectivity in protein families Science 286 1999 295 299
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 74
    • 78049307619 scopus 로고    scopus 로고
    • Crystallographic and nuclear magnetic resonance evaluation of the impact of peptide binding to the second PDZ domain of protein tyrosine phosphatase 1E
    • J. Zhang, P.J. Sapienza, H. Ke, A. Chang, S.R. Hengel, and H. Wang Crystallographic and nuclear magnetic resonance evaluation of the impact of peptide binding to the second PDZ domain of protein tyrosine phosphatase 1E Biochemistry 49 2010 9280 9291
    • (2010) Biochemistry , vol.49 , pp. 9280-9291
    • Zhang, J.1    Sapienza, P.J.2    Ke, H.3    Chang, A.4    Hengel, S.R.5    Wang, H.6
  • 75
    • 33845186553 scopus 로고    scopus 로고
    • Demonstration of long-range interactions in a PDZ domain by NMR, kinetics, and protein engineering
    • S. Gianni, T. Walma, A. Arcovito, N. Calosci, A. Bellelli, and A. Engström Demonstration of long-range interactions in a PDZ domain by NMR, kinetics, and protein engineering Structure 14 2006 1801 1809
    • (2006) Structure , vol.14 , pp. 1801-1809
    • Gianni, S.1    Walma, T.2    Arcovito, A.3    Calosci, N.4    Bellelli, A.5    Engström, A.6
  • 77
    • 77249178809 scopus 로고    scopus 로고
    • Conserved tertiary couplings stabilize elements in the PDZ fold, leading to characteristic patterns of domain conformational flexibility
    • B.K. Ho, and D.A. Agard Conserved tertiary couplings stabilize elements in the PDZ fold, leading to characteristic patterns of domain conformational flexibility Protein Sci. 19 2010 398 411
    • (2010) Protein Sci. , vol.19 , pp. 398-411
    • Ho, B.K.1    Agard, D.A.2
  • 79
    • 84859332583 scopus 로고    scopus 로고
    • Conformational dynamics and thermodynamics of protein-ligand binding studied by NMR relaxation
    • M. Akke Conformational dynamics and thermodynamics of protein-ligand binding studied by NMR relaxation Biochem. Soc. Trans. 40 2012 419 423
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 419-423
    • Akke, M.1
  • 80
    • 33846582419 scopus 로고    scopus 로고
    • Energetics of peptide recognition by the second PDZ domain of human protein tyrosine phosphatase 1E
    • S. Milev, S. Bjelić, O. Georgiev, and I. Jelesarov Energetics of peptide recognition by the second PDZ domain of human protein tyrosine phosphatase 1E Biochemistry 46 2007 1064 1078
    • (2007) Biochemistry , vol.46 , pp. 1064-1078
    • Milev, S.1    Bjelić, S.2    Georgiev, O.3    Jelesarov, I.4
  • 81
    • 34249679667 scopus 로고    scopus 로고
    • A thermodynamic ligand binding study of the third PDZ domain (PDZ3) from the mammalian neuronal protein PSD-95
    • D.L.T. Saro, C. Rupasinghe, A. Paredes, N. Caspers, and M.R. Spaller A thermodynamic ligand binding study of the third PDZ domain (PDZ3) from the mammalian neuronal protein PSD-95 Biochemistry 46 2007 6340 6352
    • (2007) Biochemistry , vol.46 , pp. 6340-6352
    • Saro, D.L.T.1    Rupasinghe, C.2    Paredes, A.3    Caspers, N.4    Spaller, M.R.5
  • 82
    • 0036088602 scopus 로고    scopus 로고
    • The linkage between protein folding and functional cooperativity: Two sides of the same coin?
    • I. Luque, S.A. Leavitt, and E. Freire The linkage between protein folding and functional cooperativity: two sides of the same coin? Annu. Rev. Biophys. Biomol. Struct. 31 2002 235 256
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 235-256
    • Luque, I.1    Leavitt, S.A.2    Freire, E.3
  • 83
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • V.J. Hilser, and E.B. Thompson Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins Proc. Natl Acad. Sci. USA 104 2007 8311 8315
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 84
    • 79959670454 scopus 로고    scopus 로고
    • The INAD scaffold is a dynamic, redox-regulated modulator of signaling in the Drosophila eye
    • W. Liu, W. Wen, Z. Wei, J. Yu, F. Ye, and C.H. Liu The INAD scaffold is a dynamic, redox-regulated modulator of signaling in the Drosophila eye Cell 145 2011 1088 1101
    • (2011) Cell , vol.145 , pp. 1088-1101
    • Liu, W.1    Wen, W.2    Wei, Z.3    Yu, J.4    Ye, F.5    Liu, C.H.6
  • 85
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulse field gradients
    • M. Sattler, J. Schleucher, and C. Greisinger Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulse field gradients Prog. Nucl. Magn. Reson. Spectrosc. 34 1999 93 158
    • (1999) Prog. Nucl. Magn. Reson. Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Greisinger, C.3
  • 89
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • B.A. Johnson Using NMRView to visualize and analyze the NMR spectra of macromolecules Methods Mol. Biol. 278 2004 313 352
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 90
    • 33746248741 scopus 로고    scopus 로고
    • Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assignment
    • Keller, R. (2004). Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assignment. ETH.
    • (2004) ETH
    • Keller, R.1
  • 91
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • P. Güntert, C. Mumenthaler, and K. Wüthrich Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 273 1997 283 298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 92
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from β-spectrin
    • M. Nilges, M.J. Macias, S.I. O'Donoghue, and H. Oschkinat Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from β-spectrin J. Mol. Biol. 269 1997 408 422
    • (1997) J. Mol. Biol. , vol.269 , pp. 408-422
    • Nilges, M.1    Macias, M.J.2    O'Donoghue, S.I.3    Oschkinat, H.4
  • 93


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.