Catalytic domain of ADAM33 and methods of use thereof

Details Catalytic domain of ADAM33 and methods of use thereof Catalytic domain of ADAM33 and methods of use thereof

2007-04-24

2007-04-24

Nashed, Nashaat T. (Department: 1656)

Chemistry: molecular biology and microbiology

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

Hydrolase

C435S069100, C435S252300, C435S320100, C435S471000

Reexamination Certificate

active

10741204

ABSTRACT:
The present invention discloses purified polypeptides that comprise an active ADAM33 catalytic domain. In addition, the present invention discloses nucleic acids that encode the polypeptides of the present invention. The present invention also discloses methods of growing X-ray diffractable crystals of polypeptides comprising the active ADAM33 catalytic domain. In addition, the present invention discloses methods of using the X-ray diffractable crystals of ADAM33 in structure-based drug design to identify compounds that can modulate the enzymatic activity of ADAM33. The present invention also discloses methods of treating respiratory disorders by administering therapeutic amounts of the ADAM33 catalytic domain.

REFERENCES:
patent: 5830742 (1998-11-01), Black et al.
patent: 6013466 (2000-01-01), Black et al.
patent: 6420154 (2002-07-01), Sheppard et al.
patent: 6683165 (2004-01-01), Keith et al.
patent: 6762044 (2004-07-01), Sheppard et al.
patent: 6927056 (2005-08-01), Todd et al.
patent: 2002/0172670 (2002-11-01), Rose et al.
patent: 2003/0138925 (2003-07-01), Keith et al.
patent: 2003/0235882 (2003-12-01), Shimkets et al.
patent: 2004/0002470 (2004-01-01), Keith et al.
patent: 2004/0018970 (2004-01-01), Shimkets et al.
patent: 2004/0023215 (2004-02-01), Keith et al.
patent: 2004/0077011 (2004-04-01), Keith et al.
patent: 2004/0091473 (2004-05-01), DuBose et al.
patent: 2004/0152869 (2004-08-01), Zhang et al.
patent: 2004/0157309 (2004-08-01), Orth et al.
patent: WO 03/031594 (2003-04-01), None
Yamamoto-Katayama, S., et al., 2001, “Site-directed removal of N-glycosylation sites in BST-1/CD157: Effects on molecular and functional heterogeneity”, Biochemical Journal, vol. 357, pp. 385-392.
Armour, Augustin, et al., “The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs,” FEBS Letters 524:154-8 (2002).
Black, Roy A., et al., “A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells,”Nature385:729-33 (1997).
Bottomley, Kevin M., et al., “Matrix metalloproteinases and the potential therapeutic role for matrix metalloproteinase inhibitors in Chronic Obstructive Pulmonary Disease (COPD),”Annual Reports in Medicinal Chemistry37:209-16 (2002).
Coombs, Gary S., et al., “Substrate specificity of prostate-specific antigen (PSA),”Chemistry&Biology5:475-488 (1998).
Drazen, Jeffrey M., et al., “Inherit the wheeze,”Nature418:383-4 (2002).
Fernandez-Catalan, Carlos, et al., “Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinase-2, the soluble progelatinase A receptor,”The EMBO Journal17:5238-48 (1998).
Gearing, A.J.H., et al., “Processing of tumor necrosis factor-α precursor by metalloproteinases,”Nature370:555-7 (1994).
Gomis-Rüth, Franz-Xaver, et al., “Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1,”Nature389:77-81 (1997).
Gunn, Teresa M., et al., “Identification and preliminary characterization of mouseAdam33,” BMC Genetics 3:1-8 (2002).
Hogate, ST, et al., “ADAM 33: just another asthma gene or a breakthrough in understanding the origins of bronchial hyperresponsiveness?”Thorax58:466-9 (2003).
Houghten, Richard A., et al., “Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery,”Nature354:84-6 (1991).
Lee, Meng-Huee, et al., “Mapping and characterization of the functional epitopes of tissue inhibitor of metalloproteinases (TIMP)-3 using TIMP-1 as the scaffold: A new frontier in TIMP engineering,”Protein Science11:2493-2503 (2002).
Lind, Denise L., et al., “ADAM33is not associated with asthma in Puerto Rican or Mexican Populations,”American Journal of Respiratory and Critical Care Medicine168:1312-16 2003).
Maskos, Klaus, et al., “Crystal structure of the catalytic domain of human tumor necrosis factor-α-converting enzyme,”Proc. Natl. Acad. Sci.95:3408-12 (1998).
Matthews, David J., et al., “Substrate phage: selection of protease substrates by monovalent phage display,”Science260:1113-7 (1993).
Matthews, David J., et al., “A survey of furin substrate specificity using substrate phage display,”Protein Science3:1197-1205 (1994).
McGeehan, Gerard M., et al., “Regulation of tumour necrosis factor-α processing by a metalloproteinase inhibitor,”Nature370:558-61 (1994).
Milla, Marcos E., et al., “Specific sequence elements are required for the expression of funcional tumor necrosis factor-α-converting enzyme (TACE),” The Journal of Biological Chemistry 274:30563-70 (1999).
Mohan, Mohita J., et al., “The tumor necrosis factor-α converting enzyme (TACE): a unique metalloproteinase with highly defined substrate selectivity,”Biochemistry41:9462-69 (2002).
Mohler, Kendall M., et al., “Protection against a lethal dose of endotoxin by an inhibitor of tumour necrosis factor processing,”Nature370:218-220 (1994).
Morgunova, Ekaterina, et al., “Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed,”Science284:1667-70 (1999).
Morris, David G., et al., “Loss of integrin ανβ6-mediated TGF-β activation causes Mmp12-dependent emphysema,”Nature422:169-73 (2003).
Nagase, Hideaki, “Activation Mechanisms of Matrix Metalloproteinases,”Biol. Chem.378:151-160 (1997).
Nagase, Hideaki, et al., “Matrix metalloproteinases,”The Journal of Biological Chemistry274:21491-4 (1999).
Orth, Peter, et al. “Crystal structure of the catalytic domain of human ADAM33,”J. Mol. Biol.335:129-37 (2004).
Polgár, László, “Metalloproteases,” Mechanisms of Protease Action, CRC Press, Inc., Boca Raton, Florida pp. 183-218 (1989).
Postma, D.S., et al., “ADAM33gene: confirming a gene without linkage,”Clin. Exp. Allergy34:1-3 (2004).
Roberts, Anita B., “Smoke signals for lung disease,”Nature422:130-1 (2003).
Shapiro, Steven D., et al., “ADAM-33Surfaces as an Asthma Gene,”N Engl J Med347:936-8 (2002).
Smutzer, Gregory, “Molecular Demolition,”The Scientist16:34 (2002).
Turk, Benjamin E., et al., “Determination of protease cleavage site motifs using mixture-based oriented peptide libraries,”Nature Biotechnology19:661-7 (2001).
Van Eerdewegh, Paul, et al., “Association of theADAM33gene with asthma and bronchial hyperresponsiveness,”Nature418:426-30 (2002).
Werner, M., et al., “Asthma is associated with single-nucleotide polymorphisms inADAM33,” Clin Exp Allergy34:26-31 (2004).
Yoshinaka, Tsuyoshi, et al., “Identification and characterization of novel mouse and human ADAM33s with potential metalloprotease activity,”Gene282:227-36 (2002).
Prosise et al., Protease domain of human ADAM33 produced by Drosophila S2 cells. Protein Expr Purif. Dec. 2004;38(2):292-301.
Orth et al., Crystal structure of the catalytic domain of human ADAM33. J Mol Biol. Jan. 2, 2004;335(1):129-37.

Affiliated with

Also associated with

Rating

Catalytic domain of ADAM33 and methods of use thereof does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Catalytic domain of ADAM33 and methods of use thereof, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Catalytic domain of ADAM33 and methods of use thereof will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3743766