Crystal structure of the catalytic domain of human DUSP5, a dual specificity MAP kinase protein phosphatase

Proteins: Structure, Function and Genetics

Volumn 66, Issue 1, 2007, Pages 253-258

  Jeong, Dae Gwin ^a   Cho, Yoon Hea ^a   Yoon, Tae Sung ^a   Kim, Jae Hoon ^a,b   Ryu, Seong Eon ^a   Kim, Seung Jun ^a  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^b Jeju National University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DUAL SPECIFICITY PHOSPHATASE 5; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATASE;

AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; CATALYSIS; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; X RAY DIFFRACTION;

CATALYTIC DOMAIN; HUMANS; MITOGEN-ACTIVATED PROTEIN KINASES; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN-TYROSINE-PHOSPHATASE;

EID: 33845610511     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21224     Document Type: Article

References (28)

1. Chang L, Karin M. Mammalian MAP kinase signalling cascades. Nature 2001;410:37-40.
2. Camps M, Nichols A, Arkinstall S. Dual specificity phosphatases: a gene family for control of MAP kinase function. FASEB J 2000;14:6-16.
3. Zhang ZY. Protein tyrosine phosphatases: structure and function, substrate specificity, and inhibitor development. Annu Rev Pharmacol Toxicol 2002;42:209-234.
4. Alonso A, Sasin J, Bottini N, Friedberg I, Friedberg I, Osterman A, Godzik A, Hunter T, Dixon J, Mustelin T. Protein tyrosine phosphatases in the human genome. Cell 2004;117:699-711.
5. Farooq A, Zhou MM. Structure and regulation of MAPK phosphatases. Cell Signal 2004;16:769-779.
6. Kwak SP, Dixon JE. Multiple dual specificity protein tyrosine phosphatases are expressed and regulated differentially in liver cell lines. J Biol Chem 1995;270:1156-1160.
7. Ueda K, Arakawa H, Nakamura Y. Dual-specificity phosphatase 5 (DUSP5) as a direct transcriptional target of tumor suppressor p53. Oncogene 2003;22:5586-5591.
8. Farooq A, Plotnikova O, Chaturvedi G, Yan S, Zeng L, Zhang Q, Zhou MM. Solution structure of the MAPK phosphatase PAC1 catalytic domain. Structure 2003;11:155-164.
9. Stewart AE, Dowd S, Keyse SM, McDonald NQ. Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation. Nat Struct Biol 1999;6:174-181.
10. Leslie AG. Integration of macromolecular diffraction data. Acta Crystallogr D Biol Crystallogr 1999;55:1696-1702.
11. CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
12. Kissinger CR, Gehlhaar DK, Fogel DB. Rapid automated molecular replacement by evolutionary search. Acta Crystallogr D Biol Crystallogr 1999;55:484-491.
13. Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 1998;54:905-921.
14. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
15. Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PRO-CHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993;26:283-291.
16. Carson M. Ribbons. Macromolecular crystallography. Methods Enzymol 1997;227:493-505.
17. Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.
18. Esnouf RM. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J Mol Graph Model 1997;15:132-134.
19. Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991;24:946-950.
20. Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
21. Yuvaniyama J, Denu JM, Dixon JE, Saper MA. Crystal structure of the dual specificity protein phosphatase VHR. Science 1996;272:1328-1331.
22. Song H, Hanlon N, Brown NR, Noble ME, Johnson LN, Barford D. Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2. Mol Cell 2001;7:615-626.
23. Lee JO, Yang H, Georgescu MM, Di Cristofano A, Maehama T, Shi Y, Dixon JE, Pandolfi P, Pavletich NP. Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell 1999;99:323-334.
24. Changela A, Ho CK, Martins A, Shuman S, Móndragon A. Structure and mechanism of the RNA triphosphatase comonent of mammalian mRNA capping enzyme. EMBO J 2001;20:2575-2586.
25. Camps M, Nichols A, Gillieron C, Antonsson B, Muda M, Chabert C, Boschert U, Arkinstall S. Catalytic activation of the phosphatase MKP3 by ERK2 mitogen-activated protein kinase. Science 1998;280:1262-1265.
26. Mandl M, Slack DN, Keyse SM. Specific inactivation and nuclear anchoring of extracellular signal-regulated kinase 2 by the inducible dual-specificity protein phophatase DUSP5. Mol Cell Biol 2005;25:1830-1845.
27. Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE. Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution. Nat Struct Biol 1998;5:400-406.
28. Changela A, Martins A, Shuman S, Mondragon A. Crystal structure of baculovirus RNA triphosphatase complexed with phosphate. J Biol Chem 2005;280:17848-17856.