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Volumn 76, Issue 2-3, 1998, Pages 334-340

Effect of peptide binding on amide proton exchange rates in the PDZ2 domain from human phosphatase hPTP1E

Author keywords

Amide exchange; Ligand binding; NMR; PDZ2 from hPTP1E

Indexed keywords

PHOSPHATASE;

EID: 0032453619     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o98-069     Document Type: Article
Times cited : (7)

References (30)
  • 2
    • 0026455190 scopus 로고
    • Kinetics of amide proton exchange in parvalbumin studied by 1H 2-D NMR
    • Baldellon, C., Padilla, A., and Cavé, A. 1992. Kinetics of amide proton exchange in parvalbumin studied by 1H 2-D NMR. Biochimie (Paris), 74: 837-844.
    • (1992) Biochimie (Paris) , vol.74 , pp. 837-844
    • Baldellon, C.1    Padilla, A.2    Cavé, A.3
  • 3
    • 0028026907 scopus 로고
    • A novel protein-tyrosine phosphatase with homology to both the cytoskeletal proteins of the band 4.1 family and junction-associated guanylate kinases
    • Banville, D., Ahmad, S., Stocco, R., and Shen, S.-H. 1994. A novel protein-tyrosine phosphatase with homology to both the cytoskeletal proteins of the band 4.1 family and junction-associated guanylate kinases. J. Biol. Chem. 269: 22 320-22 327.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22320-22327
    • Banville, D.1    Ahmad, S.2    Stocco, R.3    Shen, S.-H.4
  • 4
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced hetronuclear spectroscopy
    • Bodenhausen, G., and Ruben, D.J. 1980. Natural abundance nitrogen-15 NMR by enhanced hetronuclear spectroscopy. Chem. Phys. Lett. 69: 185-189.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 5
    • 0031960011 scopus 로고    scopus 로고
    • Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition
    • Daniels, D.L., Cohen, A.R., Anderson, J.M., and Brünger, A.T. 1998. Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition. Nat. Struct. Biol. 5: 317-325.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 317-325
    • Daniels, D.L.1    Cohen, A.R.2    Anderson, J.M.3    Brünger, A.T.4
  • 6
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle, D.A., Lee, A., Lewis, J., Kim, E., Sheng, M., and MacKinnon, R. 1996. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell, 85: 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
  • 7
    • 0032174747 scopus 로고    scopus 로고
    • Main-chain signal assignment for the PDZ2 domain from human protein tyrosine phosphatase hPTP1E and its complex with a C-terminal peptide from the Fas receptor
    • In press
    • Ekiel, I., Banville, D., Shen, S.-H., Slon-Usakiewicz, J.J., Koshy, A., and Gehring, K. 1998. Main-chain signal assignment for the PDZ2 domain from human protein tyrosine phosphatase hPTP1E and its complex with a C-terminal peptide from the Fas receptor. J. Biomol. NMR. In press.
    • (1998) J. Biomol. NMR.
    • Ekiel, I.1    Banville, D.2    Shen, S.-H.3    Slon-Usakiewicz, J.J.4    Koshy, A.5    Gehring, K.6
  • 9
    • 0030293766 scopus 로고    scopus 로고
    • Protein-protein interactions: PDZ domain networks
    • Fanning, A.S., and Anderson, J.M. 1996. Protein-protein interactions: PDZ domain networks. Curr. Biol. 6: 1386-1388.
    • (1996) Curr. Biol. , vol.6 , pp. 1386-1388
    • Fanning, A.S.1    Anderson, J.M.2
  • 11
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt, A., and Nielsen, S.O. 1966. Hydrogen exchange in proteins. Adv. Protein Chem. 21: 287-386.
    • (1966) Adv. Protein Chem. , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 12
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau, H.C., Schenker, L.T., Kennedy, M.B., and Seeburg, P.H. 1995. Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science (Washington, D.C.), 269: 1737-1740.
    • (1995) Science (Washington, D.C.) , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 14
    • 0027384196 scopus 로고
    • Hydrogen exchange in unligated and ligated staphylococcal nuclease
    • Loh, S.N., Prehoda, K.E., Wang, J., and Markley, J.L. 1993. Hydrogen exchange in unligated and ligated staphylococcal nuclease. Biochemistry, 32: 11 022-11 028.
    • (1993) Biochemistry , vol.32 , pp. 11022-11028
    • Loh, S.N.1    Prehoda, K.E.2    Wang, J.3    Markley, J.L.4
  • 15
    • 0028040007 scopus 로고
    • Molecular cloning of a novel protein-tyrosine phosphatase containing a membrane-binding domain and GLGF repeats
    • Maekawa, K., Imagawa, N., Nagamatsu, M., and Harada, S. 1994. Molecular cloning of a novel protein-tyrosine phosphatase containing a membrane-binding domain and GLGF repeats. FEBS Lett. 337: 200-206.
    • (1994) FEBS Lett. , vol.337 , pp. 200-206
    • Maekawa, K.1    Imagawa, N.2    Nagamatsu, M.3    Harada, S.4
  • 16
    • 0026455196 scopus 로고
    • Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR
    • Mayne, L., Patterson, Y., Cerasoli, D., and Englander, S.W. 1992. Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR. Biochemistry, 31: 10 678-10 685.
    • (1992) Biochemistry , vol.31 , pp. 10678-10685
    • Mayne, L.1    Patterson, Y.2    Cerasoli, D.3    Englander, S.W.4
  • 18
    • 0028236501 scopus 로고
    • Hydrogen-deuterium exchange in the free and immunoglobulin G-bound protein G B-domain
    • Orban, J., Alexander, P., and Bryan, P. 1994. Hydrogen-deuterium exchange in the free and immunoglobulin G-bound protein G B-domain. Biochemistry, 33: 5702-5710.
    • (1994) Biochemistry , vol.33 , pp. 5702-5710
    • Orban, J.1    Alexander, P.2    Bryan, P.3
  • 19
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C.N. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131: 266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 20
    • 0025142485 scopus 로고
    • An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR
    • Paterson, Y., Englander, S.W., and Roder, H. 1990. An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR. Science (Washington, D.C.), 249: 755-759.
    • (1990) Science (Washington, D.C.) , vol.249 , pp. 755-759
    • Paterson, Y.1    Englander, S.W.2    Roder, H.3
  • 21
    • 0026951903 scopus 로고
    • Gradient-taylored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. 1992. Gradient-taylored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR, 2: 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 22
    • 0031171361 scopus 로고    scopus 로고
    • PDZ domains: Targeting signalling molecules to sub-memranous sites
    • Ponting, C.P., Phillips, C., Davies, K.E., and Blake, D.J. 1997. PDZ domains: targeting signalling molecules to sub-memranous sites. BioEssays, 19: 469-479.
    • (1997) BioEssays , vol.19 , pp. 469-479
    • Ponting, C.P.1    Phillips, C.2    Davies, K.E.3    Blake, D.J.4
  • 24
    • 0030473797 scopus 로고    scopus 로고
    • PDZ domains bind carboxy-terminal sequences of target proteins
    • Saras, J., and Heldin, C.-H. 1996. PDZ domains bind carboxy-terminal sequences of target proteins. Trends Biochem. Sci. 21: 455-458.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 455-458
    • Saras, J.1    Heldin, C.-H.2
  • 25
    • 0028003644 scopus 로고
    • Cloning and characterization of PTPL1, a protein tyrosine phosphatase with similarities to cytoskeletal-associated proteins
    • Saras, J., Claesson-Welsh, L., Heldin, C.H., and Gonez, L.J. 1994. Cloning and characterization of PTPL1, a protein tyrosine phosphatase with similarities to cytoskeletal-associated proteins. J. Biol. Chem. 269: 24 082-24 089.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24082-24089
    • Saras, J.1    Claesson-Welsh, L.2    Heldin, C.H.3    Gonez, L.J.4
  • 26
    • 0029066512 scopus 로고
    • FAP-1: A protein tyrosine phosphatase that associates with Fas
    • Sato, T., Irie, S., Kitada, S., and Reed, J.C. 1995. FAP-1: a protein tyrosine phosphatase that associates with Fas. Science (Washington, D.C.), 268: 411-415.
    • (1995) Science (Washington, D.C.) , vol.268 , pp. 411-415
    • Sato, T.1    Irie, S.2    Kitada, S.3    Reed, J.C.4
  • 29
    • 0029968247 scopus 로고    scopus 로고
    • Global changes in amide hydrogen exchange rates for a protein antigen in complex with three different antibodies
    • Williams, D.C., Jr., Benjamin, D.C., Poljak, R.J., and Rule, G.S. 1996. Global changes in amide hydrogen exchange rates for a protein antigen in complex with three different antibodies. J. Mol. Biol. 257: 866-876.
    • (1996) J. Mol. Biol. , vol.257 , pp. 866-876
    • Williams D.C., Jr.1    Benjamin, D.C.2    Poljak, R.J.3    Rule, G.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.