메뉴 건너뛰기




Volumn 426, Issue 24, 2014, Pages 3985-4001

Structural and mechanistic insights into the interaction between Pyk2 and paxillin LD motifs

Author keywords

cell adhesion and signaling; dynamic complex; focal adhesion kinase; paxillin binding; proline rich tyrosine kinase 2

Indexed keywords

ASPARTIC ACID; FOCAL ADHESION KINASE 2; LEUCINE; PAXILLIN; AVIAN PROTEIN; PROTEIN BINDING;

EID: 84914709169     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.08.014     Document Type: Article
Times cited : (12)

References (71)
  • 1
    • 0029154733 scopus 로고
    • Protein tyrosine kinase PYK2 involved in Ca(2 +)-induced regulation of ion channel and MAP kinase functions
    • S. Lev, H. Moreno, R. Martinez, P. Canoll, E. Peles, and J.M. Musacchio Protein tyrosine kinase PYK2 involved in Ca(2 +)-induced regulation of ion channel and MAP kinase functions Nature 376 1995 737 745
    • (1995) Nature , vol.376 , pp. 737-745
    • Lev, S.1    Moreno, H.2    Martinez, R.3    Canoll, P.4    Peles, E.5    Musacchio, J.M.6
  • 2
    • 0029096541 scopus 로고
    • Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily
    • H. Sasaki, K. Nagura, M. Ishino, H. Tobioka, K. Kotani, and T. Sasaki Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily J Biol Chem 270 1995 21206 21219
    • (1995) J Biol Chem , vol.270 , pp. 21206-21219
    • Sasaki, H.1    Nagura, K.2    Ishino, M.3    Tobioka, H.4    Kotani, K.5    Sasaki, T.6
  • 3
    • 0028826350 scopus 로고
    • Identification and characterization of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain
    • S. Avraham, R. London, Y. Fu, S. Ota, D. Hiregowdara, and J. Li Identification and characterization of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain J Biol Chem 270 1995 27742 27751
    • (1995) J Biol Chem , vol.270 , pp. 27742-27751
    • Avraham, S.1    London, R.2    Fu, Y.3    Ota, S.4    Hiregowdara, D.5    Li, J.6
  • 4
    • 0010233279 scopus 로고    scopus 로고
    • Activation of a novel calcium-dependent protein-tyrosine kinase. Correlation with c-Jun N-terminal kinase but not mitogen-activated protein kinase activation
    • H. Yu, X. Li, G.S. Marchetto, R. Dy, D. Hunter, and B. Calvo Activation of a novel calcium-dependent protein-tyrosine kinase. Correlation with c-Jun N-terminal kinase but not mitogen-activated protein kinase activation J Biol Chem 271 1996 29993 29998
    • (1996) J Biol Chem , vol.271 , pp. 29993-29998
    • Yu, H.1    Li, X.2    Marchetto, G.S.3    Dy, R.4    Hunter, D.5    Calvo, B.6
  • 5
    • 0029978069 scopus 로고    scopus 로고
    • Molecular cloning and assignment of FAK2, a novel human focal adhesion kinase, to 8p11.2-p22 by nonisotopic in situ hybridization
    • H. Herzog, J. Nicholl, Y.J. Hort, G.R. Sutherland, and J. Shine Molecular cloning and assignment of FAK2, a novel human focal adhesion kinase, to 8p11.2-p22 by nonisotopic in situ hybridization Genomics 32 1996 484 486
    • (1996) Genomics , vol.32 , pp. 484-486
    • Herzog, H.1    Nicholl, J.2    Hort, Y.J.3    Sutherland, G.R.4    Shine, J.5
  • 6
    • 33748046499 scopus 로고    scopus 로고
    • Reduced NMDA receptor tyrosine phosphorylation in PTPalpha-deficient mouse synaptosomes is accompanied by inhibition of four src family kinases and Pyk2: An upstream role for PTPalpha in NMDA receptor regulation
    • H.T. Le, L. Maksumova, J. Wang, and C.J. Pallen Reduced NMDA receptor tyrosine phosphorylation in PTPalpha-deficient mouse synaptosomes is accompanied by inhibition of four src family kinases and Pyk2: an upstream role for PTPalpha in NMDA receptor regulation J Neurochem 98 2006 1798 1809
    • (2006) J Neurochem , vol.98 , pp. 1798-1809
    • Le, H.T.1    Maksumova, L.2    Wang, J.3    Pallen, C.J.4
  • 7
    • 34347359742 scopus 로고    scopus 로고
    • The significance of proline-rich tyrosine kinase2 (Pyk2) on hepatocellular carcinoma progression and recurrence
    • C.K. Sun, K.T. Ng, B.S. Sun, J.W. Ho, T.K. Lee, and I. Ng The significance of proline-rich tyrosine kinase2 (Pyk2) on hepatocellular carcinoma progression and recurrence Br J Cancer 97 2007 50 57
    • (2007) Br J Cancer , vol.97 , pp. 50-57
    • Sun, C.K.1    Ng, K.T.2    Sun, B.S.3    Ho, J.W.4    Lee, T.K.5    Ng, I.6
  • 8
    • 78649640148 scopus 로고    scopus 로고
    • TROY (TNFRSF19) is overexpressed in advanced glial tumors and promotes glioblastoma cell invasion via Pyk2-Rac1 signaling
    • V.M. Paulino, Z. Yang, J. Kloss, M.J. Ennis, B.A. Armstrong, and J.C. Loftus TROY (TNFRSF19) is overexpressed in advanced glial tumors and promotes glioblastoma cell invasion via Pyk2-Rac1 signaling Mol Cancer Res 8 2010 1558 1567
    • (2010) Mol Cancer Res , vol.8 , pp. 1558-1567
    • Paulino, V.M.1    Yang, Z.2    Kloss, J.3    Ennis, M.J.4    Armstrong, B.A.5    Loftus, J.C.6
  • 9
    • 79951678828 scopus 로고    scopus 로고
    • FLT3/ ITD regulates leukaemia cell adhesion through alpha4beta1 integrin and Pyk2 signalling
    • A. Katsumi, H. Kiyoi, A. Abe, R. Tanizaki, T. Iwasaki, and M. Kobayashi FLT3/ ITD regulates leukaemia cell adhesion through alpha4beta1 integrin and Pyk2 signalling Eur J Haematol 86 2011 191 198
    • (2011) Eur J Haematol , vol.86 , pp. 191-198
    • Katsumi, A.1    Kiyoi, H.2    Abe, A.3    Tanizaki, R.4    Iwasaki, T.5    Kobayashi, M.6
  • 10
    • 79954616437 scopus 로고    scopus 로고
    • Nephrocystin-4 regulates Pyk2-induced tyrosine phosphorylation of nephrocystin-1 to control targeting to monocilia
    • M.C. Liebau, K. Hopker, R.U. Muller, I. Schmedding, S. Zank, and B. Schairer Nephrocystin-4 regulates Pyk2-induced tyrosine phosphorylation of nephrocystin-1 to control targeting to monocilia J Biol Chem 286 2011 14237 14245
    • (2011) J Biol Chem , vol.286 , pp. 14237-14245
    • Liebau, M.C.1    Hopker, K.2    Muller, R.U.3    Schmedding, I.4    Zank, S.5    Schairer, B.6
  • 11
    • 77957802351 scopus 로고    scopus 로고
    • The Pyk2 FERM regulates Pyk2 complex formation and phosphorylation
    • D. Riggs, Z. Yang, J. Kloss, and J.C. Loftus The Pyk2 FERM regulates Pyk2 complex formation and phosphorylation Cell Signal 23 2011 288 296
    • (2011) Cell Signal , vol.23 , pp. 288-296
    • Riggs, D.1    Yang, Z.2    Kloss, J.3    Loftus, J.C.4
  • 12
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: In command and control of cell motility
    • S.K. Mitra, D.A. Hanson, and D.D. Schlaepfer Focal adhesion kinase: in command and control of cell motility Nat Rev Mol Cell Biol 6 2005 56 68
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 13
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The first ten years
    • J.T. Parsons Focal adhesion kinase: the first ten years J Cell Sci 116 2003 1409 1416
    • (2003) J Cell Sci , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 14
    • 0028889436 scopus 로고
    • Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas
    • T.R. Polte, and S.K. Hanks Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas Proc Natl Acad Sci USA 92 1995 10678 10682
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10678-10682
    • Polte, T.R.1    Hanks, S.K.2
  • 15
    • 0035985220 scopus 로고    scopus 로고
    • The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly
    • Y. Liu, J.C. Loijens, K.H. Martin, A.V. Karginov, and J.T. Parsons The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly Mol Biol Cell 13 2002 2147 2156
    • (2002) Mol Biol Cell , vol.13 , pp. 2147-2156
    • Liu, Y.1    Loijens, J.C.2    Martin, K.H.3    Karginov, A.V.4    Parsons, J.T.5
  • 16
    • 0029955660 scopus 로고    scopus 로고
    • An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase
    • J.D. Hildebrand, J.M. Taylor, and J.T. Parsons An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase Mol Cell Biol 16 1996 3169 3178
    • (1996) Mol Cell Biol , vol.16 , pp. 3169-3178
    • Hildebrand, J.D.1    Taylor, J.M.2    Parsons, J.T.3
  • 17
    • 0035809922 scopus 로고    scopus 로고
    • Regulation of CDC42 GTPase by proline-rich tyrosine kinase 2 interacting with PSGAP, a novel pleckstrin homology and Src homology 3 domain containing rhoGAP protein
    • X.R. Ren, Q.S. Du, Y.Z. Huang, S.Z. Ao, L. Mei, and W.C. Xiong Regulation of CDC42 GTPase by proline-rich tyrosine kinase 2 interacting with PSGAP, a novel pleckstrin homology and Src homology 3 domain containing rhoGAP protein J Cell Biol 152 2001 971 984
    • (2001) J Cell Biol , vol.152 , pp. 971-984
    • Ren, X.R.1    Du, Q.S.2    Huang, Y.Z.3    Ao, S.Z.4    Mei, L.5    Xiong, W.C.6
  • 18
    • 0032531732 scopus 로고    scopus 로고
    • Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK- cell migration
    • D.J. Sieg, D. Ilic, K.C. Jones, C.H. Damsky, T. Hunter, and D.D. Schlaepfer Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK- cell migration EMBO J 17 1998 5933 5947
    • (1998) EMBO J , vol.17 , pp. 5933-5947
    • Sieg, D.J.1    Ilic, D.2    Jones, K.C.3    Damsky, C.H.4    Hunter, T.5    Schlaepfer, D.D.6
  • 19
    • 0030944686 scopus 로고    scopus 로고
    • Paxillin is tyrosine-phosphorylated by and preferentially associates with the calcium-dependent tyrosine kinase in rat liver epithelial cells
    • X. Li, and H.S. Earp Paxillin is tyrosine-phosphorylated by and preferentially associates with the calcium-dependent tyrosine kinase in rat liver epithelial cells J Biol Chem 272 1997 14341 14348
    • (1997) J Biol Chem , vol.272 , pp. 14341-14348
    • Li, X.1    Earp, H.S.2
  • 20
    • 0029856623 scopus 로고    scopus 로고
    • The related adhesion focal tyrosine kinase forms a complex with paxillin in hematopoietic cells
    • R. Salgia, S. Avraham, E. Pisick, J.L. Li, S. Raja, and E.A. Greenfield The related adhesion focal tyrosine kinase forms a complex with paxillin in hematopoietic cells J Biol Chem 271 1996 31222 31226
    • (1996) J Biol Chem , vol.271 , pp. 31222-31226
    • Salgia, R.1    Avraham, S.2    Pisick, E.3    Li, J.L.4    Raja, S.5    Greenfield, E.A.6
  • 21
    • 0031025122 scopus 로고    scopus 로고
    • The related adhesion focal tyrosine kinase is tyrosine-phosphorylated after beta1-integrin stimulation in B cells and binds to p130cas
    • A. Astier, H. Avraham, S.N. Manie, J. Groopman, T. Canty, and S. Avraham The related adhesion focal tyrosine kinase is tyrosine-phosphorylated after beta1-integrin stimulation in B cells and binds to p130cas J Biol Chem 272 1997 228 232
    • (1997) J Biol Chem , vol.272 , pp. 228-232
    • Astier, A.1    Avraham, H.2    Manie, S.N.3    Groopman, J.4    Canty, T.5    Avraham, S.6
  • 22
    • 0029770721 scopus 로고    scopus 로고
    • Activation of Pyk2 by stress signals and coupling with JNK signaling pathway
    • G. Tokiwa, I. Dikic, S. Lev, and J. Schlessinger Activation of Pyk2 by stress signals and coupling with JNK signaling pathway Science 273 1996 792 794
    • (1996) Science , vol.273 , pp. 792-794
    • Tokiwa, G.1    Dikic, I.2    Lev, S.3    Schlessinger, J.4
  • 23
    • 0026759309 scopus 로고
    • Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • J.L. Guan, and D. Shalloway Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation Nature 358 1992 690 692
    • (1992) Nature , vol.358 , pp. 690-692
    • Guan, J.L.1    Shalloway, D.2
  • 25
    • 42049113411 scopus 로고    scopus 로고
    • Compensatory role for Pyk2 during angiogenesis in adult mice lacking endothelial cell FAK
    • S.M. Weis, S.T. Lim, K.M. Lutu-Fuga, L.A. Barnes, X.L. Chen, and J.R. Gothert Compensatory role for Pyk2 during angiogenesis in adult mice lacking endothelial cell FAK J Cell Biol 181 2008 43 50
    • (2008) J Cell Biol , vol.181 , pp. 43-50
    • Weis, S.M.1    Lim, S.T.2    Lutu-Fuga, K.M.3    Barnes, L.A.4    Chen, X.L.5    Gothert, J.R.6
  • 26
    • 67349236641 scopus 로고    scopus 로고
    • Crystal structures of free and ligand-bound focal adhesion targeting domain of Pyk2
    • J. Lulo, S. Yuzawa, and J. Schlessinger Crystal structures of free and ligand-bound focal adhesion targeting domain of Pyk2 Biochem Biophys Res Commun 383 2009 347 352
    • (2009) Biochem Biophys Res Commun , vol.383 , pp. 347-352
    • Lulo, J.1    Yuzawa, S.2    Schlessinger, J.3
  • 27
    • 0034851713 scopus 로고    scopus 로고
    • Inhibition of PYK2-induced actin cytoskeleton reorganization, PYK2 autophosphorylation and focal adhesion targeting by FAK
    • Q.S. Du, X.R. Ren, Y. Xie, Q. Wang, L. Mei, and W.C. Xiong Inhibition of PYK2-induced actin cytoskeleton reorganization, PYK2 autophosphorylation and focal adhesion targeting by FAK J Cell Sci 114 2001 2977 2987
    • (2001) J Cell Sci , vol.114 , pp. 2977-2987
    • Du, Q.S.1    Ren, X.R.2    Xie, Y.3    Wang, Q.4    Mei, L.5    Xiong, W.C.6
  • 29
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin: Adapting to change
    • M.C. Brown, and C.E. Turner Paxillin: adapting to change Physiol Rev 84 2004 1315 1339
    • (2004) Physiol Rev , vol.84 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2
  • 30
    • 0033539801 scopus 로고    scopus 로고
    • Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
    • S. Liu, S.M. Thomas, D.G. Woodside, D.M. Rose, W.B. Kiosses, and M. Pfaff Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses Nature 402 1999 676 681
    • (1999) Nature , vol.402 , pp. 676-681
    • Liu, S.1    Thomas, S.M.2    Woodside, D.G.3    Rose, D.M.4    Kiosses, W.B.5    Pfaff, M.6
  • 31
    • 73949141711 scopus 로고    scopus 로고
    • Paxillin-kinase-linker tyrosine phosphorylation regulates directional cell migration
    • J.A. Yu, N.O. Deakin, and C.E. Turner Paxillin-kinase-linker tyrosine phosphorylation regulates directional cell migration Mol Biol Cell 20 2009 4706 4719
    • (2009) Mol Biol Cell , vol.20 , pp. 4706-4719
    • Yu, J.A.1    Deakin, N.O.2    Turner, C.E.3
  • 32
    • 50249107474 scopus 로고    scopus 로고
    • Paxillin comes of age
    • N.O. Deakin, and C.E. Turner Paxillin comes of age J Cell Sci 121 2008 2435 2444
    • (2008) J Cell Sci , vol.121 , pp. 2435-2444
    • Deakin, N.O.1    Turner, C.E.2
  • 33
    • 0033577810 scopus 로고    scopus 로고
    • Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling
    • C.E. Turner, M.C. Brown, J.A. Perrotta, M.C. Riedy, S.N. Nikolopoulos, and A.R. McDonald Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling J Cell Biol 145 1999 851 863
    • (1999) J Cell Biol , vol.145 , pp. 851-863
    • Turner, C.E.1    Brown, M.C.2    Perrotta, J.A.3    Riedy, M.C.4    Nikolopoulos, S.N.5    McDonald, A.R.6
  • 34
    • 0029827130 scopus 로고    scopus 로고
    • Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding
    • M.C. Brown, J.A. Perrotta, and C.E. Turner Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding J Cell Biol 135 1996 1109 1123
    • (1996) J Cell Biol , vol.135 , pp. 1109-1123
    • Brown, M.C.1    Perrotta, J.A.2    Turner, C.E.3
  • 35
    • 0033579448 scopus 로고    scopus 로고
    • The role of focal adhesion kinase binding in the regulation of tyrosine phosphorylation of paxillin
    • J.W. Thomas, M.A. Cooley, J.M. Broome, R. Salgia, J.D. Griffin, and C.R. Lombardo The role of focal adhesion kinase binding in the regulation of tyrosine phosphorylation of paxillin J Biol Chem 274 1999 36684 36692
    • (1999) J Biol Chem , vol.274 , pp. 36684-36692
    • Thomas, J.W.1    Cooley, M.A.2    Broome, J.M.3    Salgia, R.4    Griffin, J.D.5    Lombardo, C.R.6
  • 36
    • 84901706706 scopus 로고    scopus 로고
    • How to find a leucine in a haystack? Structure, ligand recognition and regulation of leucine-aspartic acid (LD) motifs
    • T. Alam, M. Alazmi, X. Gao, and S.T. Arold How to find a leucine in a haystack? Structure, ligand recognition and regulation of leucine-aspartic acid (LD) motifs Biochem J 460 2014 317 329
    • (2014) Biochem J , vol.460 , pp. 317-329
    • Alam, T.1    Alazmi, M.2    Gao, X.3    Arold, S.T.4
  • 37
  • 39
    • 1542289014 scopus 로고    scopus 로고
    • NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: Evidence for a two-site binding model
    • G. Gao, K.C. Prutzman, M.L. King, D.M. Scheswohl, E.F. DeRose, and R.E. London NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model J Biol Chem 279 2004 8441 8451
    • (2004) J Biol Chem , vol.279 , pp. 8441-8451
    • Gao, G.1    Prutzman, K.C.2    King, M.L.3    Scheswohl, D.M.4    Derose, E.F.5    London, R.E.6
  • 41
    • 14144252115 scopus 로고    scopus 로고
    • Structural features of the focal adhesion kinase-paxillin complex give insight into the dynamics of focal adhesion assembly
    • C.M. Bertolucci, C.D. Guibao, and J. Zheng Structural features of the focal adhesion kinase-paxillin complex give insight into the dynamics of focal adhesion assembly Protein Sci 14 2005 644 652
    • (2005) Protein Sci , vol.14 , pp. 644-652
    • Bertolucci, C.M.1    Guibao, C.D.2    Zheng, J.3
  • 43
    • 49649120467 scopus 로고    scopus 로고
    • GIT1 paxillin-binding domain is a four-helix bundle, and it binds to both paxillin LD2 and LD4 motifs
    • Z.M. Zhang, J.A. Simmerman, C.D. Guibao, and J.J. Zheng GIT1 paxillin-binding domain is a four-helix bundle, and it binds to both paxillin LD2 and LD4 motifs J Biol Chem 283 2008 18685 18693
    • (2008) J Biol Chem , vol.283 , pp. 18685-18693
    • Zhang, Z.M.1    Simmerman, J.A.2    Guibao, C.D.3    Zheng, J.J.4
  • 44
  • 45
    • 0031585990 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels
    • J.R. Gillespie, and D. Shortle Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels J Mol Biol 268 1997 158 169
    • (1997) J Mol Biol , vol.268 , pp. 158-169
    • Gillespie, J.R.1    Shortle, D.2
  • 46
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • M. Strong, M.R. Sawaya, S. Wang, M. Phillips, D. Cascio, and D. Eisenberg Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis Proc Natl Acad Sci USA 103 2006 8060 8065
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8060-8065
    • Strong, M.1    Sawaya, M.R.2    Wang, S.3    Phillips, M.4    Cascio, D.5    Eisenberg, D.6
  • 47
    • 77951623055 scopus 로고    scopus 로고
    • Super-resolution biomolecular crystallography with low-resolution data
    • G.F. Schroder, M. Levitt, and A.T. Brunger Super-resolution biomolecular crystallography with low-resolution data Nature 464 2010 1218 1222
    • (2010) Nature , vol.464 , pp. 1218-1222
    • Schroder, G.F.1    Levitt, M.2    Brunger, A.T.3
  • 48
    • 20444393525 scopus 로고    scopus 로고
    • Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds
    • P. Schanda, and B. Brutscher Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds J Am Chem Soc 127 2005 8014 8015
    • (2005) J Am Chem Soc , vol.127 , pp. 8014-8015
    • Schanda, P.1    Brutscher, B.2
  • 49
    • 0035859852 scopus 로고    scopus 로고
    • NMR-detected order in core residues of denatured bovine pancreatic trypsin inhibitor
    • E. Barbar, M. Hare, M. Makokha, G. Barany, and C. Woodward NMR-detected order in core residues of denatured bovine pancreatic trypsin inhibitor Biochemistry 40 2001 9734 9742
    • (2001) Biochemistry , vol.40 , pp. 9734-9742
    • Barbar, E.1    Hare, M.2    Makokha, M.3    Barany, G.4    Woodward, C.5
  • 50
    • 1842531458 scopus 로고    scopus 로고
    • IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution
    • T.B. Green, O. Ganesh, K. Perry, L. Smith, L.H. Phylip, and T.M. Logan IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution Biochemistry 43 2004 4071 4081
    • (2004) Biochemistry , vol.43 , pp. 4071-4081
    • Green, T.B.1    Ganesh, O.2    Perry, K.3    Smith, L.4    Phylip, L.H.5    Logan, T.M.6
  • 51
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • K. Pervushin, R. Riek, G. Wider, and K. Wuthrich Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution Proc Natl Acad Sci USA 94 1997 12366 12371
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 52
    • 0032496229 scopus 로고    scopus 로고
    • Leupaxin is a novel LIM domain protein that forms a complex with PYK2
    • B.P. Lipsky, C.R. Beals, and D.E. Staunton Leupaxin is a novel LIM domain protein that forms a complex with PYK2 J Biol Chem 273 1998 11709 11713
    • (1998) J Biol Chem , vol.273 , pp. 11709-11713
    • Lipsky, B.P.1    Beals, C.R.2    Staunton, D.E.3
  • 55
    • 0036197382 scopus 로고    scopus 로고
    • Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase
    • G. Liu, C.D. Guibao, and J. Zheng Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase Mol Cell Biol 22 2002 2751 2760
    • (2002) Mol Cell Biol , vol.22 , pp. 2751-2760
    • Liu, G.1    Guibao, C.D.2    Zheng, J.3
  • 57
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling Biophys J 78 2000 1606 1619
    • (2000) Biophys J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 58
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • P. Schuck, M.A. Perugini, N.R. Gonzales, G.J. Howlett, and D. Schubert Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems Biophys J 82 2002 1096 1111
    • (2002) Biophys J , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 59
    • 46249118974 scopus 로고    scopus 로고
    • Measuring protein-protein interactions by equilibrium sedimentation
    • [Chapter 18:Unit]
    • A. Balbo, P.H. Brown, E.H. Braswell, and P. Schuck Measuring protein-protein interactions by equilibrium sedimentation Curr Protoc Immunol 2007 [Chapter 18:Unit]
    • (2007) Curr Protoc Immunol
    • Balbo, A.1    Brown, P.H.2    Braswell, E.H.3    Schuck, P.4
  • 61
    • 0028282555 scopus 로고
    • Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation
    • N.A. Farrow, R. Muhandiram, A.U. Singer, S.M. Pascal, C.M. Kay, and G. Gish Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation Biochemistry 33 1994 5984 6003
    • (1994) Biochemistry , vol.33 , pp. 5984-6003
    • Farrow, N.A.1    Muhandiram, R.2    Singer, A.U.3    Pascal, S.M.4    Kay, C.M.5    Gish, G.6
  • 63
    • 0029881450 scopus 로고    scopus 로고
    • The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase
    • S. Grzesiek, A. Bax, G.M. Clore, A.M. Gronenborn, J.S. Hu, and J. Kaufman The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase Nat Struct Biol 3 1996 340 345
    • (1996) Nat Struct Biol , vol.3 , pp. 340-345
    • Grzesiek, S.1    Bax, A.2    Clore, G.M.3    Gronenborn, A.M.4    Hu, J.S.5    Kaufman, J.6
  • 64
    • 0030936560 scopus 로고    scopus 로고
    • Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme i of the Escherichia coli phosphotransferase system
    • D.S. Garrett, Y.J. Seok, A. Peterkofsky, G.M. Clore, and A.M. Gronenborn Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system Biochemistry 36 1997 4393 4398
    • (1997) Biochemistry , vol.36 , pp. 4393-4398
    • Garrett, D.S.1    Seok, Y.J.2    Peterkofsky, A.3    Clore, G.M.4    Gronenborn, A.M.5
  • 65
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor 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
  • 69
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • P. Emsley, and K. Cowtan Coot: model-building tools for molecular graphics Acta Crystallogr D Biol Crystallogr 60 2004 2126 2132
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.