Skip to main content
Log in

Solution Structure of the Second PDZ Domain of the Neuronal Adaptor X11α and its Interaction with the C-terminal Peptide of the Human Copper Chaperone for Superoxide Dismutase

  • Article
  • Published:
Journal of Biomolecular NMR Aims and scope Submit manuscript

Abstract

Protection against reactive oxygen species is provided by the copper containing enzyme superoxide dismutase 1 (SOD1). The copper chaperone CCS is responsible for copper insertion into apo-SOD1. This role is impaired by an interaction between the second PDZ domain (PDZ2α) of the neuronal adaptor protein X11α and the third domain of CCS (McLoughlin et al. (2001) J. Biol. Chem., 276, 9303–9307). The solution structure of the PDZ2α domain has been determined and the interaction with peptides derived from CCS has been explored. PDZ2α binds to the last four amino acids of the CCS protein (PAHL) with a dissociation constant of 91 ± 2 μM. Peptide variants have been used to map the interaction areas on PDZ2α for each amino acid, showing an important role for the C-terminal leucine, in line with canonical PDZ-peptide interactions.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

CCS:

copper chaperone for SOD1

HOAc:

acetic acid

PDZ:

post-synaptic density 95, Drosophila disks-large, Zona occludens 1

RP-HPLC:

reversed phase high-performance liquid chromatography

SOD1:

superoxide dismutase 1

References

  • T. Biederer X.W. Cao T.C. Sudhof X.R. Liu (2002) J. Neurosci. 22 7340–7351

    Google Scholar 

  • G. Birrane J. Chung J.A.A. Ladias (2003) J. Biol. Chem. 278 1399–1402 Occurrence Handle10.1074/jbc.C200571200 Occurrence Handle12444095

    Article  PubMed  Google Scholar 

  • A. Brünger (1992) X-PLOR, version 3.1. A system for X-ray crystallography and NMR Yale University Press New Haven, CT

    Google Scholar 

  • S. Butz M. Okamoto T.C. Sudhof (1998) Cell 94 773–782 Occurrence Handle10.1016/S0092-8674(00)81736-5 Occurrence Handle9753324

    Article  PubMed  Google Scholar 

  • C. Cai S.K. Coleman K. Niemi K. Keinanen (2002) J. Biol. Chem. 277 31484–31490 Occurrence Handle10.1074/jbc.M204354200 Occurrence Handle12070168

    Article  PubMed  Google Scholar 

  • B.P.C. Chen T.W. Hai (1994) Gene 139 73–75 Occurrence Handle10.1016/0378-1119(94)90525-8 Occurrence Handle8112591

    Article  PubMed  Google Scholar 

  • G. Cornilescu F. Delaglio A. Bax (1999) J. Biomol. NMR 13 289–302 Occurrence Handle10.1023/A:1008392405740 Occurrence Handle10212987

    Article  PubMed  Google Scholar 

  • V.C. Culotta L.W.J. Klomp J. Strain R.L.B. Casareno B. Krems J.D. Gitlin (1997) J. Biol. Chem. 272 23469–23472 Occurrence Handle10.1074/jbc.272.38.23469 Occurrence Handle9295278

    Article  PubMed  Google Scholar 

  • F. Delaglio S. Grzesiek G.W. Vuister G. Zhu J. Pfeifer A. Bax (1995) J. Biomol. NMR 6 277–293 Occurrence Handle10.1007/BF00197809 Occurrence Handle8520220

    Article  PubMed  Google Scholar 

  • D.A. Doyle A. Lee J. Lewis E. Kim M. Sheng R. MacKinnon (1996) Cell 85 1067–1076 Occurrence Handle10.1016/S0092-8674(00)81307-0 Occurrence Handle8674113

    Article  PubMed  Google Scholar 

  • M. Falconi M. Iovino A. Desideri (1999) Structure 7 903–908 Occurrence Handle10.1016/S0969-2126(99)80117-8 Occurrence Handle10467139

    Article  PubMed  Google Scholar 

  • A.S. Fanning J.M. Anderson (1999) J. Clin. Invest. 103 767–772 Occurrence Handle10079096

    PubMed  Google Scholar 

  • W. Feng J.S. Fan M. Jiang Y.W. Shi M. Zhang (2002) J. Biol. Chem. 277 41140–41146 Occurrence Handle10.1074/jbc.M207206200 Occurrence Handle12196542

    Article  PubMed  Google Scholar 

  • W. Feng Y.W. Shi M. Li M.J. Zhang (2003) Nat. Struct. Biol. 10 972–978 Occurrence Handle10.1038/nsb992 Occurrence Handle14555997

    Article  PubMed  Google Scholar 

  • R. Fogh J. Ionides E. Ulrich W. Boucher W. Vranken J.P. Linge W. Rieping T.N. Bhat J. Westbrook K. Henrick G. Gilliland H. Berman J. Thornton M. Nilges J. Markley E. Laue (2002) Nat. Struct. Biol. 9 416–418 Occurrence Handle10.1038/nsb0602-416 Occurrence Handle12032555

    Article  PubMed  Google Scholar 

  • P. Guntert C. Mumenthaler K. Wuthrich (1997) J. Mol. Biol. 273 283–298 Occurrence Handle10.1006/jmbi.1997.1284 Occurrence Handle9367762

    Article  PubMed  Google Scholar 

  • B.Z. Harris B.J. Hillier W.A. Lim (2001) Biochemistry (Mosc). 40 5921–5930 Occurrence Handle10.1021/bi010142l

    Article  Google Scholar 

  • M.D. Harrison C.E. Jones C.T. Dameron (1999) J. Biol. Inorg. Chem. 4 145–153 Occurrence Handle10.1007/s007750050297 Occurrence Handle10499084

    Article  PubMed  Google Scholar 

  • M. Helgstrand P. Kraulis P. Allard T. Hard (2000) J. Biomol. NMR 18 329–336

    Google Scholar 

  • T. Herrmann P. Guntert K. Wuthrich (2002) J. Mol. Biol. 319 209–227 Occurrence Handle10.1016/S0022-2836(02)00241-3 Occurrence Handle12051947

    Article  PubMed  Google Scholar 

  • B.J. Hillier K.S. Christopherson K.E. Prehoda D.S. Bredt W.A. Lim (1999) Science 284 812–815 Occurrence Handle10.1126/science.284.5415.812 Occurrence Handle10221915

    Article  PubMed  Google Scholar 

  • C.S. Ho V. Marinescu M.L. Steinhilb J.R. Gaut R.S. Turner E.L. Stuenkel (2002) J. Biol. Chem. 277 27021–27028 Occurrence Handle10.1074/jbc.M201823200 Occurrence Handle12016213

    Article  PubMed  Google Scholar 

  • Y.J. Im J.H. Lee S.H. Park S.J. Park S.H. Rho G.B. Kang E. Kim S.H. Eom (2003) J. Biol. Chem. 278 48099–48104 Occurrence Handle10.1074/jbc.M306919200 Occurrence Handle12954649

    Article  PubMed  Google Scholar 

  • B.S. Kang D.R. Cooper Y. Devedjiev U. Derewenda Z.S. Derewenda (2003) Structure 11 845–853 Occurrence Handle10.1016/S0969-2126(03)00125-4 Occurrence Handle12842047

    Article  PubMed  Google Scholar 

  • A. Kannt S. Young D.S. Bendall (1996) Biochim. Biophys. Acta 1277 115–126

    Google Scholar 

  • R. Keller (2004) The Computer Aided Resonance Assignment Tutorial CANTINA Verlag

    Google Scholar 

  • A.L. Lamb A.S. Torres T.V. O’Halloran A.C. Rosenzweig (2001) Nat. Struct. Biol. 8 751–755 Occurrence Handle10.1038/nsb0901-751 Occurrence Handle11524675

    Article  PubMed  Google Scholar 

  • A.L. Lamb A.K. Wernimont R.A. Pufahl V.C. Culotta T.V. O’Halloran A.C. Rosenzweig (1999) Nat. Struct. Biol. 6 724–729 Occurrence Handle10.1038/11489 Occurrence Handle10426947

    Article  PubMed  Google Scholar 

  • R.A. Laskowski M.W. Macarthur D.S. Moss J.M. Thornton (1993) Journal of Applied Crystallography 26 283–291 Occurrence Handle10.1107/S0021889892009944

    Article  Google Scholar 

  • J.P. Linge M.A. Williams C. Spronk A. Bonvin M. Nilges (2003) Prot.-Struc. Func. Gen. 50 496–506 Occurrence Handle10.1002/prot.10299

    Article  Google Scholar 

  • G. Lipari A. Szabo (1982a) J. Am. Chem. Soc. 104 4546–4559 Occurrence Handle10.1021/ja00381a009

    Article  Google Scholar 

  • G. Lipari A. Szabo (1982b) J. Am. Chem. Soc. 104 4559–4570 Occurrence Handle10.1021/ja00381a010

    Article  Google Scholar 

  • A.M. Mandel M. Akke A.G. Palmer (1995) J. Mol. Biol. 246 144–163 Occurrence Handle10.1006/jmbi.1994.0073 Occurrence Handle7531772

    Article  PubMed  Google Scholar 

  • D.M. McLoughlin C.L. Standen K.F. Lau S. Ackerley T.P. Bartnikas J.D. Gitlin C.C.J. Miller (2001) J. Biol. Chem. 276 9303–9307 Occurrence Handle10.1074/jbc.M010023200 Occurrence Handle11115513

    Article  PubMed  Google Scholar 

  • S.B. Nabuurs A.J. Nederveen W. Vranken J.F. Doreleijers A. Bonvin G.W. Vuister G. Vriend C. Spronk (2004) Prot.-Struc. Func. Bioinformatics 55 483–486 Occurrence Handle10.1002/prot.20118

    Article  Google Scholar 

  • T.V. O’Halloran V.C. Culotta (2000) J. Biol. Chem. 275 25057–25060 Occurrence Handle10.1074/jbc.R000006200 Occurrence Handle10816601

    Article  PubMed  Google Scholar 

  • M. Okamoto T.C. Sudhof (1997) J. Biol. Chem. 272 31459–31464 Occurrence Handle10.1074/jbc.272.50.31459 Occurrence Handle9395480

    Article  PubMed  Google Scholar 

  • A. Palmer M. Zimmer K.S. Erdmann V. Eulenburg A. Porthin R. Heumann U. Deutsch R. Klein (2002) Mol. Cell 9 725–737 Occurrence Handle10.1016/S1097-2765(02)00488-4 Occurrence Handle11983165

    Article  PubMed  Google Scholar 

  • M.M.O. Pena J. Lee D.J. Thiele (1999) J. Nutr. 129 1251–1260 Occurrence Handle10395584

    PubMed  Google Scholar 

  • T.D. Rae P.J. Schmidt R.A. Pufahl V.C. Culotta T.V. O’Halloran (1999) Science 284 805–808 Occurrence Handle10.1126/science.284.5415.805 Occurrence Handle10221913

    Article  PubMed  Google Scholar 

  • A.C. Rosenzweig T.V. O’Halloran (2000) Curr. Opin. Chem. Biol. 4 140–147 Occurrence Handle10.1016/S1367-5931(99)00066-6 Occurrence Handle10742187

    Article  PubMed  Google Scholar 

  • C.D. Schwieters J.J. Kuszewski N. Tjandra G.M. Clore (2003) J. Magn. Reson. 160 65–73 Occurrence Handle10.1016/S1090-7807(02)00014-9 Occurrence Handle12565051

    Article  PubMed  Google Scholar 

  • G.S. Tjabringa J. Aarbiou D.K. Ninaber J.W. Drijfhout O.E. Sorensen N. Borregaard K.F. Rabe P.S. Hiemstra (2003) J. Immunol. 171 6690–6696 Occurrence Handle14662872

    PubMed  Google Scholar 

  • P. Vaccaro L. Dente (2002) FEBS Lett. 512 345–346 Occurrence Handle10.1016/S0014-5793(02)02220-2 Occurrence Handle11852108

    Article  PubMed  Google Scholar 

  • L.C. van den Berk M.A. van Ham M.M. te Lindert T. Walma J. Aelen G.W. Vuister W.J. Hendriks (2004) Mol. Biol. Rep. 31 203–215 Occurrence Handle10.1007/s11033-005-1407-8 Occurrence Handle15663004

    Article  PubMed  Google Scholar 

  • M. Ham Particlevan W. Hendriks (2003) Mol. Biol. Rep. 30 69–82 Occurrence Handle10.1023/A:1023941703493 Occurrence Handle12841577

    Article  PubMed  Google Scholar 

  • G. Vriend (1990) J. Mol. Graph. 8 52–56 Occurrence Handle10.1016/0263-7855(90)80070-V Occurrence Handle2268628

    Article  PubMed  Google Scholar 

  • Walma, T. (2004) The second PDZ domain of PTP-BL, Ph.D. thesis, Radboud University of Nijmegen

  • T. Walma C.A.E.M. Spronk M. Tessari J. Aelen J. Schepens W. Hendriks G.W. Vuister (2002) J. Mol. Biol. 316 1101–1110 Occurrence Handle10.1006/jmbi.2002.5402 Occurrence Handle11884147

    Article  PubMed  Google Scholar 

  • P. Zimmermann K. Meerschaert G. Reekmans I. Leenaerts J.V. Small J. Vandekerckhove G. David J. Gettemans (2002) Mol. Cell 9 1215–1225 Occurrence Handle10.1016/S1097-2765(02)00549-X Occurrence Handle12086619

    Article  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Marcellus Ubbink.

Electronic supplementary material

Rights and permissions

Reprints and permissions

About this article

Cite this article

Duquesne, A.E., Ruijter, M.d., Brouwer, J. et al. Solution Structure of the Second PDZ Domain of the Neuronal Adaptor X11α and its Interaction with the C-terminal Peptide of the Human Copper Chaperone for Superoxide Dismutase. J Biomol NMR 32, 209–218 (2005). https://doi.org/10.1007/s10858-005-7333-1

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10858-005-7333-1

Key words

Navigation