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Volumn 12, Issue 1, 2004, Pages 11-20

A Closed Binding Pocket and Global Destabilization Modify the Binding Properties of an Alternatively Spliced Form of the Second PDZ Domain of PTP-BL

Author keywords

[No Author keywords available]

Indexed keywords

APC PROTEIN; PDZ PROTEIN; PHOSPHATASE; PROTEIN; PTP BL PROTEIN; RIL PROTEIN; UNCLASSIFIED DRUG;

EID: 1642493671     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2003.11.023     Document Type: Article
Times cited : (27)

References (46)
  • 1
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai Y., Milne J.S., Mayne L., Englander S.W. Primary structure effects on peptide group hydrogen exchange. Proteins. 17:1993;75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 2
    • 0032502332 scopus 로고    scopus 로고
    • Role of the omega-loop in the activity, substrate specificity, and structure of class a beta-lactamase
    • Banerjee S., Pieper U., Kapadia G., Pannell L.K., Herzberg O. Role of the omega-loop in the activity, substrate specificity, and structure of class A beta-lactamase. Biochemistry. 37:1998;3286-3296.
    • (1998) Biochemistry , vol.37 , pp. 3286-3296
    • Banerjee, S.1    Pieper, U.2    Kapadia, G.3    Pannell, L.K.4    Herzberg, O.5
  • 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., Shen S.H. 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. 269:1994;22320-22327.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22320-22327
    • Banville, D.1    Ahmad, S.2    Stocco, R.3    Shen, S.H.4
  • 4
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C.H., Xia T.-H., Billeter M., Güntert P., Wüthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR. 6:1995;1-10.
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.H.1    Xia, T.-H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 5
    • 0037449799 scopus 로고    scopus 로고
    • Novel mode of ligand recognition by the Erbin PDZ domain
    • Birrane G., Chung J., Ladias J.A. Novel mode of ligand recognition by the Erbin PDZ domain. J. Biol. Chem. 278:2003;1399-1402.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1399-1402
    • Birrane, G.1    Chung, J.2    Ladias, J.A.3
  • 7
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase
    • Cornilescu G., Marquardt J.L., Ottiger M., Bax A. Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase. J. Am. Chem. Soc. 120:1998;6836-6837.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.L.2    Ottiger, M.3    Bax, A.4
  • 8
    • 0030778437 scopus 로고    scopus 로고
    • No evidence for involvement of mouse protein-tyrosine phosphatase-BAS-like Fas-associated phosphatase-1 in Fas-mediated apoptosis
    • Cuppen E., Nagata S., Wieringa B., Hendriks W. No evidence for involvement of mouse protein-tyrosine phosphatase-BAS-like Fas-associated phosphatase-1 in Fas-mediated apoptosis. J. Biol. Chem. 272:1997;30215-30220.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30215-30220
    • Cuppen, E.1    Nagata, S.2    Wieringa, B.3    Hendriks, W.4
  • 9
    • 0031916105 scopus 로고    scopus 로고
    • PDZ motifs in PTP-BL and RIL bind to internal protein segments in the LIM domain protein RIL
    • Cuppen E., Gerrits H., Pepers B., Wieringa B., Hendriks W. PDZ motifs in PTP-BL and RIL bind to internal protein segments in the LIM domain protein RIL. Mol. Biol. Cell. 9:1998;671-683.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 671-683
    • Cuppen, E.1    Gerrits, H.2    Pepers, B.3    Wieringa, B.4    Hendriks, W.5
  • 10
    • 0032831897 scopus 로고    scopus 로고
    • Identification and molecular characterization of BP75, a novel bromodomain-containing protein
    • a
    • Cuppen E., van Ham M., Pepers B., Wieringa B., Hendriks W. Identification and molecular characterization of BP75, a novel bromodomain-containing protein. FEBS Lett. 459:1999;291-298. a.
    • (1999) FEBS Lett. , vol.459 , pp. 291-298
    • Cuppen, E.1    Van Ham, M.2    Pepers, B.3    Wieringa, B.4    Hendriks, W.5
  • 12
    • 0034010331 scopus 로고    scopus 로고
    • The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL
    • Cuppen E., van Ham M., Wansink D.G., de Leeuw A., Wieringa B., Hendriks W. The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL. Eur. J. Cell Biol. 79:2000;283-293.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 283-293
    • Cuppen, E.1    Van Ham, M.2    Wansink, D.G.3    De Leeuw, A.4    Wieringa, B.5    Hendriks, W.6
  • 14
    • 0034048847 scopus 로고    scopus 로고
    • Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data
    • Dosset P., Hus J.C., Blackledge M., Marion D. Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data. J. Biomol. NMR. 16:2000;23-28.
    • (2000) J. Biomol. NMR , vol.16 , pp. 23-28
    • Dosset, P.1    Hus, J.C.2    Blackledge, M.3    Marion, D.4
  • 15
    • 0034884233 scopus 로고    scopus 로고
    • A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings
    • Dosset P., Hus J.C., Marion D., Blackledge M. A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings. J. Biomol. NMR. 20:2001;223-231.
    • (2001) J. Biomol. NMR , vol.20 , pp. 223-231
    • Dosset, P.1    Hus, J.C.2    Marion, D.3    Blackledge, M.4
  • 16
    • 0032453619 scopus 로고    scopus 로고
    • Effect of peptide binding on amide proton exchange rates in the PDZ2 domain from human phosphatase hPTP1E
    • Ekiel I., Banville D., Shen S.H., Gehring K. Effect of peptide binding on amide proton exchange rates in the PDZ2 domain from human phosphatase hPTP1E. Biochem. Cell Biol. 76:1998;334-340.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 334-340
    • Ekiel, I.1    Banville, D.2    Shen, S.H.3    Gehring, K.4
  • 17
    • 0034632672 scopus 로고    scopus 로고
    • The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain
    • Erdmann K.S., Kuhlmann J., Lessmann V., Herrmann L., Eulenburg V., Muller O., Heumann R. The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain. Oncogene. 19:2000;3894-3901.
    • (2000) Oncogene , vol.19 , pp. 3894-3901
    • Erdmann, K.S.1    Kuhlmann, J.2    Lessmann, V.3    Herrmann, L.4    Eulenburg, V.5    Muller, O.6    Heumann, R.7
  • 18
    • 0037174873 scopus 로고    scopus 로고
    • PDZ7 of glutamate receptor interacting protein binds to its target via a novel hydrophobic surface area
    • Feng W., Fan J.S., Jiang M., Shi Y.W., Zhang M. PDZ7 of glutamate receptor interacting protein binds to its target via a novel hydrophobic surface area. J. Biol. Chem. 277:2002;41140-41146.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41140-41146
    • Feng, W.1    Fan, J.S.2    Jiang, M.3    Shi, Y.W.4    Zhang, M.5
  • 19
    • 0035843906 scopus 로고    scopus 로고
    • The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif
    • Gross C., Heumann R., Erdmann K.S. The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif. FEBS Lett. 496:2001;101-104.
    • (2001) FEBS Lett. , vol.496 , pp. 101-104
    • Gross, C.1    Heumann, R.2    Erdmann, K.S.3
  • 20
    • 12244288351 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in the regulation of cytokinesis
    • Herrmann L., Dittmar T., Erdmann K.S. The protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in the regulation of cytokinesis. Mol. Biol. Cell. 14:2003;230-240.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 230-240
    • Herrmann, L.1    Dittmar, T.2    Erdmann, K.S.3
  • 21
    • 0032876680 scopus 로고    scopus 로고
    • Protein conformational stabilities can be determined from hydrogen exchange rates
    • Huyghues-Despointes B.M., Scholtz J.M., Pace C.N. Protein conformational stabilities can be determined from hydrogen exchange rates. Nat. Struct. Biol. 6:1999;910-912.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 910-912
    • Huyghues-Despointes, B.M.1    Scholtz, J.M.2    Pace, C.N.3
  • 23
    • 0036301446 scopus 로고    scopus 로고
    • Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the beta2-beta3 loop to PDZ domain-ligand interactions
    • Kozlov G., Banville D., Gehring K., Ekiel I. Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the beta2-beta3 loop to PDZ domain-ligand interactions. J. Mol. Biol. 320:2002;813-820.
    • (2002) J. Mol. Biol. , vol.320 , pp. 813-820
    • Kozlov, G.1    Banville, D.2    Gehring, K.3    Ekiel, I.4
  • 24
    • 0030339738 scopus 로고    scopus 로고
    • Aqua and procheck-nmr: Programs for checking the quality of protein structures solved by nmr
    • Laskowski R.A., Rullmann J.A., MacArthur M.W., Kaptein R., Thornton J.M. Aqua and procheck-nmr. programs for checking the quality of protein structures solved by nmr J. Biomol. NMR. 8:1996;477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 25
    • 0031687653 scopus 로고    scopus 로고
    • Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design
    • Liang J., Edelsbrunner H., Woodward C. Anatomy of protein pockets and cavities. measurement of binding site geometry and implications for ligand design Protein Sci. 7:1998;1884-1897.
    • (1998) Protein Sci. , vol.7 , pp. 1884-1897
    • Liang, J.1    Edelsbrunner, H.2    Woodward, C.3
  • 27
    • 0033555678 scopus 로고    scopus 로고
    • Association of protein-tyrosine phosphatase PTP-BAS with the transcription-factor-inhibitory protein IkappaBalpha through interaction between the PDZ1 domain and ankyrin repeats
    • Maekawa K., Imagawa N., Naito A., Harada S., Yoshie O., Takagi S. Association of protein-tyrosine phosphatase PTP-BAS with the transcription-factor-inhibitory protein IkappaBalpha through interaction between the PDZ1 domain and ankyrin repeats. Biochem. J. 337:1999;179-184.
    • (1999) Biochem. J. , vol.337 , pp. 179-184
    • Maekawa, K.1    Imagawa, N.2    Naito, A.3    Harada, S.4    Yoshie, O.5    Takagi, S.6
  • 28
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel A.M., Akke M., Palmer A.G. 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, A.G.3
  • 29
    • 0031976414 scopus 로고    scopus 로고
    • Solution structure and dynamics of a designed monomeric variant of the lambda Cro repressor
    • Mossing M.C. Solution structure and dynamics of a designed monomeric variant of the lambda Cro repressor. Protein Sci. 7:1998;983-993.
    • (1998) Protein Sci. , vol.7 , pp. 983-993
    • Mossing, M.C.1
  • 31
    • 0037009284 scopus 로고    scopus 로고
    • Investigation of the PDZ domain ligand binding site using chemically modified peptides
    • Novak K.A., Fujii N., Guy R.K. Investigation of the PDZ domain ligand binding site using chemically modified peptides. Bioorg. Med. Chem. Lett. 12:2002;2471-2474.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 2471-2474
    • Novak, K.A.1    Fujii, N.2    Guy, R.K.3
  • 33
    • 0026566796 scopus 로고
    • Analysis of insertions/deletions in protein structures
    • Pascarella S., Argos P. Analysis of insertions/deletions in protein structures. J. Mol. Biol. 224:1992;461-471.
    • (1992) J. Mol. Biol. , vol.224 , pp. 461-471
    • Pascarella, S.1    Argos, P.2
  • 34
    • 0037474545 scopus 로고    scopus 로고
    • Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase
    • Ramasubbu N., Ragunath C., Mishra P.J. Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase. J. Mol. Biol. 325:2003;1061-1076.
    • (2003) J. Mol. Biol. , vol.325 , pp. 1061-1076
    • Ramasubbu, N.1    Ragunath, C.2    Mishra, P.J.3
  • 35
    • 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., Gonez L.J. Cloning and characterization of PTPL1, a protein tyrosine phosphatase with similarities to cytoskeletal-associated proteins. J. Biol. Chem. 269:1994;24082-24089.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24082-24089
    • Saras, J.1    Claesson-Welsh, L.2    Heldin, C.H.3    Gonez, L.J.4
  • 36
    • 0030763619 scopus 로고    scopus 로고
    • A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1
    • Saras J., Franzen P., Aspenstrom P., Hellman U., Gonez L.J., Heldin C.H. A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1. J. Biol. Chem. 272:1997;24333-24338.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24333-24338
    • Saras, J.1    Franzen, P.2    Aspenstrom, P.3    Hellman, U.4    Gonez, L.J.5    Heldin, C.H.6
  • 37
    • 0029066512 scopus 로고
    • FAP-1: A protein tyrosine phosphatase that associates with fas
    • Sato T., Irie S., Kitada S., Reed J.C. FAP-1. a protein tyrosine phosphatase that associates with fas Science. 268:1995;411-415.
    • (1995) Science , vol.268 , pp. 411-415
    • Sato, T.1    Irie, S.2    Kitada, S.3    Reed, J.C.4
  • 38
    • 0036219167 scopus 로고    scopus 로고
    • Improving the quality of protein structures determined by NMR spectroscopy
    • Spronk C.A., Linge J.P., Hilbers C.W., Vuister G.W. Improving the quality of protein structures determined by NMR spectroscopy. J. Biomol. NMR. 22:2002;281-289.
    • (2002) J. Biomol. NMR , vol.22 , pp. 281-289
    • Spronk, C.A.1    Linge, J.P.2    Hilbers, C.W.3    Vuister, G.W.4
  • 39
    • 0037070149 scopus 로고    scopus 로고
    • PDZ domains: Troubles in classification
    • Vaccaro P., Dente L. PDZ domains. troubles in classification FEBS Lett. 512:2002;345-349.
    • (2002) FEBS Lett. , vol.512 , pp. 345-349
    • Vaccaro, P.1    Dente, L.2
  • 40
  • 41
    • 0038714883 scopus 로고    scopus 로고
    • Cloning and characterization of mCRIP2, a mouse LIM-only protein that interacts with PDZ domain IV of PTP-BL
    • van Ham M., Croes H., Schepens J., Fransen J., Wieringa B., Hendriks W. Cloning and characterization of mCRIP2, a mouse LIM-only protein that interacts with PDZ domain IV of PTP-BL. Genomics. 8:2003;631-644.
    • (2003) Genomics , vol.8 , pp. 631-644
    • Van Ham, M.1    Croes, H.2    Schepens, J.3    Fransen, J.4    Wieringa, B.5    Hendriks, W.6
  • 42
    • 0030462974 scopus 로고    scopus 로고
    • Protein structural plasticity exemplified by insertion and deletion mutants in T4 lysozyme
    • Vetter I.R., Baase W.A., Heinz D.W., Xiong J.P., Snow S., Matthews B.W. Protein structural plasticity exemplified by insertion and deletion mutants in T4 lysozyme. Protein Sci. 5:1996;2399-2415.
    • (1996) Protein Sci. , vol.5 , pp. 2399-2415
    • Vetter, I.R.1    Baase, W.A.2    Heinz, D.W.3    Xiong, J.P.4    Snow, S.5    Matthews, B.W.6
  • 43
    • 0025398721 scopus 로고
    • What if: A molecular modeling and drug design program
    • , 29
    • Vriend G. What if. a molecular modeling and drug design program J. Mol. Graph. 8:1990;52-56. , 29.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1


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