메뉴 건너뛰기




Volumn 17, Issue 9, 2008, Pages 1531-1541

Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

Author keywords

Dimerization; Dynamics; NMR; Stability; Ultracentrifuge; WW domain

Indexed keywords

ASPARTIC ACID; GLUTAMIC ACID; LEUCINE; MEMBRANE ASSOCIATED GUANYLATE KINASE; MONOMER; PHOSPHOTRANSFERASE; PROTEIN; SALVADOR PROTEIN 1; SERINE; UNCLASSIFIED DRUG;

EID: 50049112150     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.035329.108     Document Type: Article
Times cited : (7)

References (27)
  • 2
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F., and Bax, A. 1999. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13: 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 3
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 5
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Güntert, P. 2004. Automated NMR structure calculation with CYANA. Methods Mol. Biol. 278: 353-378.
    • (2004) Methods Mol. Biol , vol.278 , pp. 353-378
    • Güntert, P.1
  • 6
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., Mumenthaler, C., and Wüthrich, K. 1997. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273: 283-298.
    • (1997) J. Mol. Biol , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 7
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • Herrmann, T., Guntert, P., and Wüthrich, K. 2002. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J. Biomol. NMR 24: 171-189.
    • (2002) J. Biomol. NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wüthrich, K.3
  • 9
    • 34250793476 scopus 로고    scopus 로고
    • Influence of hPin1 WW N-terminal domain boundaries on function, protein stability, and folding
    • Jäger, M., Nguyen, H., Dendle, M., Gruebele, M., and Kelly, J.W. 2007. Influence of hPin1 WW N-terminal domain boundaries on function, protein stability, and folding. Protein Sci. 16: 1495-1501.
    • (2007) Protein Sci , vol.16 , pp. 1495-1501
    • Jäger, M.1    Nguyen, H.2    Dendle, M.3    Gruebele, M.4    Kelly, J.W.5
  • 10
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson, B.A. and Blevins, R.A. 1994. NMRView: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4: 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 11
    • 0037155792 scopus 로고    scopus 로고
    • Determinants of ligand specificity in groups I and IV WW domains as studied by surface plasmon resonance and model building
    • Kato, Y., Ito, M., Kawai, K., Nagata, K., and Tanokura, M. 2002. Determinants of ligand specificity in groups I and IV WW domains as studied by surface plasmon resonance and model building. J. Biol. Chem. 277: 10173-10177.
    • (2002) J. Biol. Chem , vol.277 , pp. 10173-10177
    • Kato, Y.1    Ito, M.2    Kawai, K.3    Nagata, K.4    Tanokura, M.5
  • 12
    • 3843151562 scopus 로고    scopus 로고
    • Common mechanism of ligand recognition by group II/III WW domains: Redefining their functional classification
    • Kato, Y., Nagata, K., Takahashi, M., Lian, L., Herrero, J.J., Sudol, M., and Tanokura, M. 2004. Common mechanism of ligand recognition by group II/III WW domains: Redefining their functional classification. J. Biol. Chem. 279: 31833-31841.
    • (2004) J. Biol. Chem , vol.279 , pp. 31833-31841
    • Kato, Y.1    Nagata, K.2    Takahashi, M.3    Lian, L.4    Herrero, J.J.5    Sudol, M.6    Tanokura, M.7
  • 13
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay, B.K., Williamson, M.P., and Sudol, M. 2000. The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14: 231-241.
    • (2000) FASEB J , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 14
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • Kigawa, T., Yabuki, T., Yoshida, Y., Tsutsui, M., Ito, Y., Shibata, T., and Yokoyama, S. 1999. Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett. 442: 15-19.
    • (1999) FEBS Lett , vol.442 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3    Tsutsui, M.4    Ito, Y.5    Shibata, T.6    Yokoyama, S.7
  • 15
    • 34547923673 scopus 로고    scopus 로고
    • KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies
    • Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Güntert, P., Kigawa, T., and Yokoyama, S. 2007. KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies. J. Biomol. NMR 39: 31-52.
    • (2007) J. Biomol. NMR , vol.39 , pp. 31-52
    • Kobayashi, N.1    Iwahara, J.2    Koshiba, S.3    Tomizawa, T.4    Tochio, N.5    Güntert, P.6    Kigawa, T.7    Yokoyama, S.8
  • 16
    • 0032939806 scopus 로고    scopus 로고
    • WW: An isolated three-stranded antiparallel β-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state
    • Koepf, E.K., Petrassi, H.M., Sudol, M., and Kelly, J.W. 1999. WW: An isolated three-stranded antiparallel β-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state. Protein Sci. 8: 841-853.
    • (1999) Protein Sci , vol.8 , pp. 841-853
    • Koepf, E.K.1    Petrassi, H.M.2    Sudol, M.3    Kelly, J.W.4
  • 18
    • 0001071357 scopus 로고    scopus 로고
    • Tuning the free-energy landscape of a WW domain by temperature, mutation, and truncation
    • Nguyen, H., Jäger, M., Moretto, A., Gruebele, M., and Kelly, J.W. 2003. Tuning the free-energy landscape of a WW domain by temperature, mutation, and truncation. Proc. Natl. Acad. Sci. 100: 3948-3953.
    • (2003) Proc. Natl. Acad. Sci , vol.100 , pp. 3948-3953
    • Nguyen, H.1    Jäger, M.2    Moretto, A.3    Gruebele, M.4    Kelly, J.W.5
  • 20
    • 0030424581 scopus 로고    scopus 로고
    • Structure and function of the WW domain
    • Sudol, M. 1996. Structure and function of the WW domain. Prog. Biophys. Mol. Biol. 65: 113-132.
    • (1996) Prog. Biophys. Mol. Biol , vol.65 , pp. 113-132
    • Sudol, M.1
  • 21
    • 0029146950 scopus 로고
    • Characterization of a novel protein-binding module - the WW domain
    • Sudol, M., Chen, H.I., Bougeret, C., Einbond, A., and Bork, P. 1995. Characterization of a novel protein-binding module - the WW domain. FEBS Lett. 369: 67-71.
    • (1995) FEBS Lett , vol.369 , pp. 67-71
    • Sudol, M.1    Chen, H.I.2    Bougeret, C.3    Einbond, A.4    Bork, P.5
  • 22
    • 0037162714 scopus 로고    scopus 로고
    • Salvador promotes both cell cycle exit and apoptosis in Drosophila and is mutated in human cancer cell lines
    • Tapon, N., Harvey, K.F., Bell, D.W., Wahrer, D.C., Schiripo, T.A., Haber, D.A., and Hariharan, I.K. 2002. Salvador promotes both cell cycle exit and apoptosis in Drosophila and is mutated in human cancer cell lines. Cell 110: 467-478.
    • (2002) Cell , vol.110 , pp. 467-478
    • Tapon, N.1    Harvey, K.F.2    Bell, D.W.3    Wahrer, D.C.4    Schiripo, T.A.5    Haber, D.A.6    Hariharan, I.K.7
  • 23
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 25
    • 0141616617 scopus 로고    scopus 로고
    • Hippo promotes proliferation arrest and apoptosis in the Salvador/Warts pathway
    • Udan, R.S., Kango-Singh, M., Nolo, R., Tao, C., and Halder, G. 2003. Hippo promotes proliferation arrest and apoptosis in the Salvador/Warts pathway. Nat. Cell Biol. 5: 914-920.
    • (2003) Nat. Cell Biol , vol.5 , pp. 914-920
    • Udan, R.S.1    Kango-Singh, M.2    Nolo, R.3    Tao, C.4    Halder, G.5
  • 26
    • 0036928101 scopus 로고    scopus 로고
    • Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40
    • Wiesner, S., Stier, G., Sattler, M., and Macias, M.J. 2002. Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40. J. Mol. Biol. 324: 807-822.
    • (2002) J. Mol. Biol , vol.324 , pp. 807-822
    • Wiesner, S.1    Stier, G.2    Sattler, M.3    Macias, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.