ERK2 crystals

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Transferase other than ribonuclease

Reexamination Certificate

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Reexamination Certificate

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11233581

ABSTRACT:
The present invention relates to crystals of the ERK2 polypeptide and complexes thereof which are useful, inter alia, for structure assisted drug design.

REFERENCES:
Canagarajah et al. Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell vol. 90, 859-869 (1997).
Fox et al. A single amino acid substitution makes ERK2 susceptible to pyridinyl imidazol inhibitors of p38 MAP kinase. Protein Sci. 7. 2249-2255 (1998).
Zhang et al. Atomic structure of the MAP kinase ERK2 at 2.3 A resolution. Nature 367, 704-711 (1994).
Gilliland et al. Crystallization of biological macromolecules of X-ray diffraction studies. Current Opinion in Struct. Biol. 6, 595-603 (1996).
Ke et al. Crystallization of RNA and RNA-protein Complex. Methods 34, 408-414 (2004).
Weincek et al. New Strategies for protein crystal growth. Ann. Rev. Biomed. Eng. 1, 505-534 (1999).
Wang et al., Structural basis of inhibitor selectivity in MAP kinases. Structure. Sep. 15, 1998;6(9):1117-28.
Szedlacsek et al., Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation. J. Mol. Biol. Aug. 17, 2001;311(3):557-68.
Eblen et al., Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs.J. Biol. Chem. Apr. 25, 2003;278(17):14926-35. Epub Feb. 19, 2003.
Vesely et al., Inhibition of cyclin-dependent kinases by purine analogues. Eur. J. Biochem. Sep. 1, 1994;224(2):771-86.
Zhang et al., Crystallization and preliminary X-ray studies of extracellular signal-regulated kinase-2/MAP kinase with an incorporated His-tag. J. Mol. Biol. Oct. 5, 1993;233(3):550-2.
Zhang et al., Activity of the MAP kinase ERK2 is controlled by a flexible surface loop. Structure. Mar. 15, 1995;3(3):299-307.

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