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Literature DB >> 15844883

Increasing the kinase specificity of k252a by protein surface recognition.

Tanya L Schneider¹, Rebecca S Mathew, Kevin P Rice, Kazuhiko Tamaki, John L Wood, Alanna Schepartz.

Abstract

[reaction: see text] Here we describe a miniature protein (1) that presents the cAMP-dependent protein kinase (PKA) recognition epitope found within the heat-stable Protein Kinase Inhibitor protein (PKI) and a miniature protein conjugate (1-K252a) in which 1 is joined covalently to the high-affinity but nonselective kinase inhibitor K252a. Miniature protein 1 recognizes PKA with an affinity that rivals that of PKI and, in the context of 1-K252a, leads to a dramatic increase in kinase specificity.

Entities: Chemical

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Year: 2005 PMID： 15844883 DOI： 10.1021/ol050179o

Source DB: PubMed Journal: Org Lett ISSN： 1523-7052 Impact factor: 6.005

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Cited

14 in total

1. Targeting diverse signaling interaction sites allows the rapid generation of bivalent kinase inhibitors.

Authors: Zachary B Hill; B Gayani K Perera; Simeon S Andrews; Dustin J Maly
Journal: ACS Chem Biol Date: 2011-12-22 Impact factor: 5.100

2. Selection of cyclic-peptide inhibitors targeting Aurora kinase A: problems and solutions.

Authors: Carolyn D Shomin; Elizabeth Restituyo; Kurt J Cox; Indraneel Ghosh
Journal: Bioorg Med Chem Date: 2011-09-29 Impact factor: 3.641

Review 3. Targeting protein-protein interactions by rational design: mimicry of protein surfaces.

Authors: Steven Fletcher; Andrew D Hamilton
Journal: J R Soc Interface Date: 2006-04-22 Impact factor: 4.118

4. Assay principle for modulators of protein-protein interactions and its application to non-ATP-competitive ligands targeting protein kinase A.

Authors: S Adrian Saldanha; Gregory Kaler; Howard B Cottam; Ruben Abagyan; Susan S Taylor
Journal: Anal Chem Date: 2006-12-15 Impact factor: 6.986

10. Staurosporine tethered peptide ligands that target cAMP-dependent protein kinase (PKA): optimization and selectivity profiling.

Authors: Carolyn D Shomin; Scott C Meyer; Indraneel Ghosh
Journal: Bioorg Med Chem Date: 2009-07-26 Impact factor: 3.641

Increasing the kinase specificity of k252a by protein surface recognition.

1. Targeting diverse signaling interaction sites allows the rapid generation of bivalent kinase inhibitors.

2. Selection of cyclic-peptide inhibitors targeting Aurora kinase A: problems and solutions.

Review 3. Targeting protein-protein interactions by rational design: mimicry of protein surfaces.

4. Assay principle for modulators of protein-protein interactions and its application to non-ATP-competitive ligands targeting protein kinase A.

5. Combined solid/solution phase synthesis of large surface area scaffolds derived from aminomethyl-benzoates.

Review 6. Bivalent inhibitors of protein kinases.

7. Synthesis of a Macrocycle Based on Linked Amino Acid Mimetics (LAAM).

8. Miniature protein ligands for EVH1 domains: interplay between affinity, specificity, and cell motility.

Review 9. The chemical biology of protein phosphorylation.

10. Staurosporine tethered peptide ligands that target cAMP-dependent protein kinase (PKA): optimization and selectivity profiling.