Methods of determining polypeptide structure and function

Details Methods of determining polypeptide structure and function Methods of determining polypeptide structure and function

2007-06-26

2007-06-26

Borin, Michael (Department: 1631)

Data processing: measuring, calibrating, or testing

Measurement system in a specific environment

Chemical analysis

C702S019000, C530S350000

Reexamination Certificate

active

10157016

ABSTRACT:
The present invention provides methods for determining the structure and/or function of one or more domains of a cation-dependent (and preferably calcium-dependent) polypeptide (particularly a calcium-dependent enzyme, which may be a protease such as calpain) in the presence of one or more cations. The invention further provides methods for identifying a ligand having the ability to bind to one or more ligand-binding domains (LBDs) of a cation-dependent (and preferably calcium-dependent) polypeptide, and ligands identified by these methods. The invention also provides methods of treating or preventing physical disorders in animals using these ligands.

REFERENCES:
Li R, et al. Structure-based design of parasitic protease inhibitors. Bioorg Med Chem. Sep. 1996;4(9):1421-7.
Hosfield CM, Elce JS, Davis PL, Jia Z. Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation. EMBO J. Dec. 15, 1999;18(24):6880-9.□□
Protein Databank SearchFields, URL=http://www.rcsb.org/pdb/cgi/queryForm.cgi.
Kellog, URL=http://www.phc.vcu.edu/Kellogg—postdoc—position.html.
Seeman, N, Current Crystallization Protocol, URL=http://seemanlab4.chem.nyu.edu
ano-pro.html.
Sorimachi, H., et al., “The Structure of Calpain.”J. Biochem.129:653-664 (2001).

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