Crystal structure of soluble glutaminyl cyclase

Details Crystal structure of soluble glutaminyl cyclase Crystal structure of soluble glutaminyl cyclase

2006-02-24

2009-08-11

Noakes, Suzanne M. (Department: 1656)

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

C435S193000, C435S231000, C435S069100

Reexamination Certificate

active

07572614

ABSTRACT:
A crystalline structure of glutaminyl cyclase (QC). is described. Also described are the methods of preparing the crystalline structure of QC and the methods for identifying candidate inhibitors of QC. In addition, a structural basis for the rational design or identification of new inhibitors that may be used to treat QC-associated disorders is also described.

REFERENCES:
patent: 6117663 (2000-09-01), Boriack-Sjodin et al.
patent: 2004/0224875 (2004-11-01), Schilling et al.
patent: 2005/0181975 (2005-08-01), Griffith et al.
patent: 2005/0202550 (2005-09-01), Pandit
patent: 2004098591 (2004-11-01), None
patent: 2004098625 (2004-11-01), None
Branden et al., “Introduction to Protein Structure Second Edition”, Garland Publishing Inc., New York, 1999.
Drenth, “Principles of X-ray Crystallography,” Springer, New York, 1995.
Kierzek et al., Biophys Chem 91:1-20, 2001.
Ngo et al., in The Protein Folding Problem and Tertiary Structure Prediction, 1994, Merz et al. (ed.), Birkhauser, Boston, MA, pp. 433 and 492-495.
Azarkan et al., Crystallization and preliminary X-ray diffraction studies of the glutaminyl cyclase fromCarica papayalatex, Acta Cryst., published online on Oct. 23, 2004, F61, p. 59-61.
Witkowski et al., Biochemistry, 38, 11643-11650, 1999.
Wishart et al., Journal of Biological Chemistry, vol. 270, No. 45, pp. 26782-26785, 1995.
Oberg, et al., “Papaya glutamine cyclase, a plant enzyme highly resistant to proteolysis, adopts an all-b conformation”, European Journal of Biochemistry, vol. 258, pp. 214-222 (1998).
Schilling, et al., “Heterologous expression and characterization of human glutaminyl cyclase: evidence for a disulfide bond with importance for catalytic activity”, Biochemistry, vol. 41, pp. 10849-10857 (2002).
Van Coille, et al., “Functional comparison of two human monocyte chemotactic protein-e isoforms, role of the amino-terminal pyroglutamic acid and processing by CD26/Dipeptidyl Peptidase IV”, Biochemistry, vol. 37, pp. 12672-12680 (1998).
Hinke, et al., “Dipeptidyl Peptidase IV (DPIC/DC26) Degradation of Glucagon”, Journal of Biological Chemistry, vol. 275, pp. 3827-3834 (2000).
Huang, et al., “Cloning, expression, characterization, and crystallization of a glutaminyl cyclase from human bone marrow: A single zinc metalloenzyme”, Protein Expression & Purification, vol. 43, pp. 65-72 (2005).
Bubsy, et al., “An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl-peptides”, The Journal of Biological Chemistry, vol. 262, No. 18, pp. 8532-8536 (1987).
Huang, et al., “Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation”, PNAS, vol. 102, No. 37, pp. 13117-13122 (2005).
Sykes, et al., “Evidence for tissue-specific forms of glutaminyl cyclase”, FEBS Letters, vol. 455, pp. 159-161 (1999).
Shilling, et al., “Identification of human glutaminyl cyclase as a metalloenzyme”, Journal of Biological Chemistry, vol. 278, pp. 29773-29779 (2003).
Fischer, et al., “Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides”, Proceedings of the national academy of sciences of the United States of America, No. 84, pp. 3628-3632 (1987).
Booth, et al., “Human glytaminyl cyclase and bacterial zinc aminopeptidase share a common fold and active site”, BMC Biology, vol. 2, No. 2 (2004).
Stewart, et al., “Role of genetic factors in the pathogenesis of osteoporosis”, Journal of Endocrinology, vol. 166, p. 235-245 (2000).
Ezura, et al., “Association of multiple nucleotide variations in the pituitary glutaminyl cyclase gene (QPCT) with low radial BMD in adult women”, Journal of Bone and Mineral Research, vol. 19, pp. 1296-1301 (2004).
Schilling, et al., “Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions”, FEBS Letters, vol. 563, pp. 191-196 (2004).
Morgan, et al., “Structure and function of amyloid in Alzheimer's disease”, Progress in Neurobiology, vol. 74, pp. 323-349 (2004).
Saido, et al., “Dominant and differential deposition of distinct beta-amyloid peptide species, A beta N3(pE), in senile plaques”, Neuron, vol. 14, pp. 457-466 (1995).
Kuo, et al., “Isolation, chemical characterization, and quantitation of a beta 3-pyroglytamyl peptide from neuritic plaques and vascular amyloid deposits”, Biochemical and Biophysical Research Communications, vol. 237, pp. 188-191 (1997).
Russo, et al., “Pyroglutamate-modified amyloid beta-peptides strongly affect cultured neuron and astrocyte survival”, Journal of Neurochemistry, vol. 82, pp. 1480-1489 (2002).
Harigaya, et al., “Amyloid beta-protein starting pyroglutamate at position 3 is a major component of the amyloid deposits in the alzheimer's disease brain”, Biochemical and Biophysical Research Communications, vol. 276, pp. 422-427 (2000).
Pawlak, Joanna et al., “Snake venom glutaminyl Cyclase,” Toxicon, 48:278-286 (2006).
Zerhouni, Samira et al., “Purification and characterization of papaya glutamine cyclotransferase, a plant enzyme highly resistance to chemical, acid and thermal denaturation,” Biochimica et Biophysica Acta, 1387:275-290 (1998).
Schilling, Stephan et al., “Heterologous Expression and Characterization of Human Glutaminyl Cyclase: Evidence for a Disulfide Bond with Importance for Catalytic Activity,” Biochemistry, 41:10849-10857 (2002).
Schilling, Stephan et al., “Substrate Specificity of Glutaminyl Cyclases from Plants and Animals,” Biol. Chem, 384:1583-1592 (Dec. 2003).
Wintjens, Rene et al., “Crystal Structure of Papaya Glutaminyl Cyclase, an Archetype for Plant and Bacterial Glutaminyl Cyclases,” J. Mol. Biol., 357:457-470 (2006).
Oberg, Keith A. et al., “Papaya glutamine cyclase, a plant enzyme highly resistant to proteolysis, adopts an all-beta conformation,” Eur. J. Biochem, 258:214-222 (1998).
Huang, Kai-Fa et al., “Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation,” PNAS, 102(37):13117-13122 (Sep. 13, 2005).

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