Crystal structure of human TMDP, a testis-specific dual specificity protein phosphatase: Implications for substrate specificity

Proteins: Structure, Function and Genetics

Volumn 66, Issue 1, 2007, Pages 239-245

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

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

^b Jeju National University   (South Korea)

Author keywords

Crystal structure; Dual specificity phosphatase; TMDP

Indexed keywords

AMINO ACID; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN TYROSINE PHOSPHATASE; TESTIS AND SKELETAL MUSCLE SPECIFIC DUAL SPECIFICITY PHOSPHATASE; THREONINE; TYROSINE; VACCINIA H1 RELATED PHOSPHATASE;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; CRYSTAL STRUCTURE; DEPHOSPHORYLATION; DOWN REGULATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; HUMAN; HYDROPHOBICITY; MOLECULAR RECOGNITION; MOLECULAR SIZE; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN MOTIF; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; SPERMATOGENESIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HELIX-LOOP-HELIX MOTIFS; HUMANS; MALE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN-TYROSINE-PHOSPHATASE; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; TESTIS; THREONINE; TYROSINE;

EID: 33845675681     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21197     Document Type: Article

References (32)

1. Zhang ZY, Zhou B, Xie L. Modulation of protein kinase signaling by protein phosphatases and inhibitors. Pharmacol Ther 2002;93:307-317.
2. Treisman R. Regulation of transcription by MAP kinase cascades. Curr Opin Cell Biol 1996;8:205-215.
3. Wu JJ, Bennett AM. Essential role for mitogen-activated protein (MAP) kinase phosphatase-1 in stress-responsive MAP kinase and cell survival signaling. J Biol Chem 2005;280:16461-16466.
4. Farooq A, Zhou MM. Structure and regulation of MAPK phosphatases. Cell Signal 2004;16:769-779.
5. 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.
6. 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.
7. Farooq A, Plotnikova O, Chaturvedi G, Yan S, Zeng L, Zhang Q, Zhou MM. Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP. Structure 2003;11:155-164.
8. Yuvaniyama J, Denu JM, Dixon JE, Saper MA. Crystal structure of the dual specificity protein phosphatase VHR. Science 1996;272:1328-1331.
9. Alonso A, Saxena M, Williams S, Mustelin T. Inhibitory role for dual specificity phosphatase VHR in T cell antigen receptor and CD28-induced Erk and Jnk activation. J Biol Chem 2001;276:4766-4771.
10. Todd JL, Rigas JD, Rafty LA, Denu JM. Dual-specificity protein tyrosine phosphatase VHR down-regulates c-Jun N-terminal kinase (JNK). Oncogene 2002;21:2573-2583.
11. Nakamura K, Shima H, Watanabe M, Haneji T, Kikuchi K. Molecular cloning and characterization of a novel dual-specificity protein phosphatase possibly involved in spermatogenesis. Biochem J 1999;344:41404-41413.
12. Nakamura K, Tanoue K, Satoh T, Takekawa M, Watanabe M, Shima H, Kikuchi K. A novel low-molecular-mass dual-specificity phosphatase. LDP-2, with a naturally occurring substitution that affects substrate specificity. J Biochem (Tokyo) 2002;132:463-470.
13. Chen HH, Luche R, Wei B, Tonks NK. Characterization of two distinct dual specificity phosphatases encoded in alternative open reading frames of a single gene located on human chromosome 10q22.2. J Biol Chem 2004;279:41404-41413.
14. Leslie AGW. Integration of macromolecular diffraction data. Acta Crystallogr Sect D 1999;55:1696-1702.
15. Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr Sect D 1994;50:760-763.
16. Kissinger CR, Gehlhaar DK, Fogel DB. Rapid automated molecular replacement by evolutionary search. Acta Crystallogr Sect D 1999;55:484-491.
17. Brunger 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 and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr Sect D 1998;54:905-921.
18. Jones TA, Zou JY, Cowan SW, Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr Sect A 1991;47:110-119.
19. Laskowski RA, Moss DS, Thornton JM. Main-chain bond lengths and bond angles in protein structures. J Appl Crystallogr 1993;26:283-291.
20. Carson M. Triggering methods in crystallographic enzyme kinetics. Presentation and analysis: illustrating structures. Methods Enzymol 1997;277:493-505.
21. Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.
22. Esnouf RM. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J Mol Graph Model 1997;15:132-134.
23. Kraulis PJ. Similarity of protein G and ubiquitin. J Appl Crystallogr 1991;24:946-950.
24. Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
25. 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.
26. Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
27. Barton GJ. Secondary structure prediction for modelling by homology. Protein Eng 1993;6:37-40.
28. Kleywegt GJ, Jones TA. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr Sect D 1994;1994;50:178-185.
29. Schumacher MA, Todd JL, Rice AE, Tanner KG, Denu JM. Structural basis for the recognition of a bisphosphorylated MAP kinase peptide by human VHR protein Phosphatase. Biochemistry 2002;41:3009-3017.
30. Camps M, Nichols A, Gillieron C, Antonsson B, Muda M, Chabert C, Boschert U, Arkinstall S. Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase. Science 1998;280:1262-1265.
31. Barford D, Flint AJ, Tonks NK. Crystal structure of human protein tyrosine phosphatase 1B. Science 1994;263:1397-1404.
32. Jia Z, Barford D, Flint AJ. Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Science 1995;268:1754-1758.