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PMID: 15782149 Published · ppublish English Evaluation Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

A rapid method for determining protein kinase phosphorylation specificity.

Nature methods ·Vol. 1 ·No. 1 ·2004-10-00 ·Pages 27-9

Hutti JE, Jarrell ET, Chang JD, Abbott DW, Storz P, Toker A, Cantley LC, Turk BE

Abstract

Selection of target substrates by protein kinases is strongly influenced by the amino acid sequence surrounding the phosphoacceptor site. Identification of the preferred peptide phosphorylation motif for a given kinase permits the production of efficient peptide substrates and greatly simplifies the mapping of phosphorylation sites in protein substrates. Here we describe a combinatorial peptide library method that allows rapid generation of phosphorylation motifs for serine/threonine kinases.

MeSH Terms
Amino Acid Motifs Binding Sites Enzyme Activation Microfluidic Analytical Techniques/methods Peptide Library Phosphorylation Protein Binding Protein Interaction Mapping/methods Protein Serine-Threonine Kinases/analysis,chemistry,metabolism Sequence Analysis, Protein/methods Substrate Specificity
Chemicals
Peptide Library Protein Serine-Threonine Kinases
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Hutti Jessica E
Division of Signal Transduction, Harvard Medical School, 330 Brookline Avenue, Boston, Massachusetts 02215, USA.
Jarrell Emily T
Chang James D
Abbott Derek W
Storz Peter
Toker Alex
Cantley Lewis C
Turk Benjamin E
Article Info
Journal
Nature methods
Abbr.
Nat Methods
ISSN
1548-7091
Published
2004-10-00
Pages
27-9
Language
English
Region
United States
NLM ID
101215604
Subset
IM
Grants
NIGMS NIH HHS · R01 GM056203 · United States
NCI NIH HHS · CA75134 · United States
NIGMS NIH HHS · GM56203 · United States
Corrections
CommentIn
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