The patent badge is an abbreviated version of the USPTO patent document. The patent badge does contain a link to the full patent document.

The patent badge is an abbreviated version of the USPTO patent document. The patent badge covers the following: Patent number, Date patent was issued, Date patent was filed, Title of the patent, Applicant, Inventor, Assignee, Attorney firm, Primary examiner, Assistant examiner, CPCs, and Abstract. The patent badge does contain a link to the full patent document (in Adobe Acrobat format, aka pdf). To download or print any patent click here.

Date of Patent:
Dec. 21, 1999

Filed:

Jan. 06, 1995
Applicant:
Inventors:

Lewis C Cantley, Cambridge, MA (US);

Zhou Songyang, Brookline, MA (US);

Assignee:

Beth Israel Hospital, Boston, MA (US);

Attorney:
Primary Examiner:
Int. Cl.
CPC ...
G01N / ; C07K / ;
U.S. Cl.
CPC ...
435-71 ; 435331 ; 436 86 ; 436518 ; 530328 ; 530329 ; 530330 ; 530331 ; 514 15 ; 514 16 ; 514 17 ; 514 18 ;
Abstract

The invention provides a method for determining an amino acid sequence motif for a phosphorylation site of a protein kinase. In the method of the invention, a protein kinase is contacted with an oriented degenerate peptide library, peptides within the library which are substrates for the kinase are converted to phosphopeptides and the phosphopeptides are separated from non-phosphorylated peptides. The isolated phosphopeptides are sequenced and an amino acid sequence motif for the phosphorylation site is determined based upon the relative abundance of different amino acids residues at each degenerate position. The invention also provides peptide substrates for protein kinase A, cell cycle control kinases (including cyclin B/p33.sup.cdc2 and cyclin A/p33.sup.CDK2), src family kinases (including pp60.sup.c-src and pp60.sup.v-src), EGF receptor, p92.sup.c-fps/fes, lck, c-abl, PDGF receptor, FGF receptor, insulin receptor, casein kinase II, NIMA kinase, phosphorylase kinase, Cam kinase II and Erk1 based upon amino acid sequence motifs for the phosphorylation sites of these kinases.


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