A rapid method for determining protein kinase phosphorylation specificity.
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.
Hutti
Jessica E
JE
Division of Signal Transduction, Harvard Medical School, 330 Brookline Avenue, Boston, Massachusetts 02215, USA.
Jarrell
Emily T
ET
Chang
James D
JD
Abbott
Derek W
DW
Storz
Peter
P
Toker
Alex
A
Cantley
Lewis C
LC
Turk
Benjamin E
BE
D020816:Amino Acid Motifs; D001665:Binding Sites; D004789:Enzyme Activation; D046210:Microfluidic Analytical Techniques / Q000379:methods*; D019151:Peptide Library; D010766:Phosphorylation; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D017346:Protein Serine-Threonine Kinases / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism*; D020539:Sequence Analysis, Protein / Q000379:methods*; D013379:Substrate Specificity
D019151:Peptide Library; D017346:Protein Serine-Threonine Kinases