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.
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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
G. Birrane J. Chung J.A.A. Ladias (2003) J. Biol. Chem. 278 1399–1402 Occurrence Handle10.1074/jbc.C200571200 Occurrence Handle12444095
A. Brünger (1992) X-PLOR, version 3.1. A system for X-ray crystallography and NMR Yale University Press New Haven, CT
S. Butz M. Okamoto T.C. Sudhof (1998) Cell 94 773–782 Occurrence Handle10.1016/S0092-8674(00)81736-5 Occurrence Handle9753324
C. Cai S.K. Coleman K. Niemi K. Keinanen (2002) J. Biol. Chem. 277 31484–31490 Occurrence Handle10.1074/jbc.M204354200 Occurrence Handle12070168
B.P.C. Chen T.W. Hai (1994) Gene 139 73–75 Occurrence Handle10.1016/0378-1119(94)90525-8 Occurrence Handle8112591
G. Cornilescu F. Delaglio A. Bax (1999) J. Biomol. NMR 13 289–302 Occurrence Handle10.1023/A:1008392405740 Occurrence Handle10212987
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
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
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
M. Falconi M. Iovino A. Desideri (1999) Structure 7 903–908 Occurrence Handle10.1016/S0969-2126(99)80117-8 Occurrence Handle10467139
A.S. Fanning J.M. Anderson (1999) J. Clin. Invest. 103 767–772 Occurrence Handle10079096
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
W. Feng Y.W. Shi M. Li M.J. Zhang (2003) Nat. Struct. Biol. 10 972–978 Occurrence Handle10.1038/nsb992 Occurrence Handle14555997
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
P. Guntert C. Mumenthaler K. Wuthrich (1997) J. Mol. Biol. 273 283–298 Occurrence Handle10.1006/jmbi.1997.1284 Occurrence Handle9367762
B.Z. Harris B.J. Hillier W.A. Lim (2001) Biochemistry (Mosc). 40 5921–5930 Occurrence Handle10.1021/bi010142l
M.D. Harrison C.E. Jones C.T. Dameron (1999) J. Biol. Inorg. Chem. 4 145–153 Occurrence Handle10.1007/s007750050297 Occurrence Handle10499084
M. Helgstrand P. Kraulis P. Allard T. Hard (2000) J. Biomol. NMR 18 329–336
T. Herrmann P. Guntert K. Wuthrich (2002) J. Mol. Biol. 319 209–227 Occurrence Handle10.1016/S0022-2836(02)00241-3 Occurrence Handle12051947
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
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
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
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
A. Kannt S. Young D.S. Bendall (1996) Biochim. Biophys. Acta 1277 115–126
R. Keller (2004) The Computer Aided Resonance Assignment Tutorial CANTINA Verlag
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
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
R.A. Laskowski M.W. Macarthur D.S. Moss J.M. Thornton (1993) Journal of Applied Crystallography 26 283–291 Occurrence Handle10.1107/S0021889892009944
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
G. Lipari A. Szabo (1982a) J. Am. Chem. Soc. 104 4546–4559 Occurrence Handle10.1021/ja00381a009
G. Lipari A. Szabo (1982b) J. Am. Chem. Soc. 104 4559–4570 Occurrence Handle10.1021/ja00381a010
A.M. Mandel M. Akke A.G. Palmer (1995) J. Mol. Biol. 246 144–163 Occurrence Handle10.1006/jmbi.1994.0073 Occurrence Handle7531772
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
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
T.V. O’Halloran V.C. Culotta (2000) J. Biol. Chem. 275 25057–25060 Occurrence Handle10.1074/jbc.R000006200 Occurrence Handle10816601
M. Okamoto T.C. Sudhof (1997) J. Biol. Chem. 272 31459–31464 Occurrence Handle10.1074/jbc.272.50.31459 Occurrence Handle9395480
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
M.M.O. Pena J. Lee D.J. Thiele (1999) J. Nutr. 129 1251–1260 Occurrence Handle10395584
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
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
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
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
P. Vaccaro L. Dente (2002) FEBS Lett. 512 345–346 Occurrence Handle10.1016/S0014-5793(02)02220-2 Occurrence Handle11852108
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
M. Ham Particlevan W. Hendriks (2003) Mol. Biol. Rep. 30 69–82 Occurrence Handle10.1023/A:1023941703493 Occurrence Handle12841577
G. Vriend (1990) J. Mol. Graph. 8 52–56 Occurrence Handle10.1016/0263-7855(90)80070-V Occurrence Handle2268628
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
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
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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
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DOI: https://doi.org/10.1007/s10858-005-7333-1