Role of amino acid residues surrounding the phosphorylation site in peptide substrates of G protein-coupled receptor kinase 2 (GRK2)

Daisuke Asai; Masaharu Murata; Riki Toita; Takahito Kawano; Hideki Nakashima; Jeong Hun Kang

doi:10.1007/s00726-016-2345-6

Role of amino acid residues surrounding the phosphorylation site in peptide substrates of G protein-coupled receptor kinase 2 (GRK2)

Daisuke Asai, Masaharu Murata, Riki Toita, Takahito Kawano, Hideki Nakashima, Jeong Hun Kang

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

A series of amino acid substitutions was made in a previously identified β-tubulin-derived GRK2 substrate peptide (⁴⁰⁴DEMEFTEAESNMN⁴¹⁶) to examine the role of amino acid residues surrounding the phosphorylation site. Anionic amino acid residues surrounding the phosphorylation site played an important role in the affinity for GRK2. Compared to the original peptide, a modified peptide (Ac-EEMEFSEAEANMN-NH₂) exhibited markedly higher affinity for GRK2, but very low affinity for GRK5, suggesting that it can be a sensitive and selective peptide for GRK2.

Original language	English
Pages (from-to)	2875-2880
Number of pages	6
Journal	Amino Acids
Volume	48
Issue number	12
DOIs	https://doi.org/10.1007/s00726-016-2345-6
Publication status	Published - Dec 1 2016

All Science Journal Classification (ASJC) codes

Biochemistry
Clinical Biochemistry
Organic Chemistry

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title = "Role of amino acid residues surrounding the phosphorylation site in peptide substrates of G protein-coupled receptor kinase 2 (GRK2)",

abstract = "A series of amino acid substitutions was made in a previously identified β-tubulin-derived GRK2 substrate peptide (404DEMEFTEAESNMN416) to examine the role of amino acid residues surrounding the phosphorylation site. Anionic amino acid residues surrounding the phosphorylation site played an important role in the affinity for GRK2. Compared to the original peptide, a modified peptide (Ac-EEMEFSEAEANMN-NH2) exhibited markedly higher affinity for GRK2, but very low affinity for GRK5, suggesting that it can be a sensitive and selective peptide for GRK2.",

author = "Daisuke Asai and Masaharu Murata and Riki Toita and Takahito Kawano and Hideki Nakashima and Kang, {Jeong Hun}",

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T1 - Role of amino acid residues surrounding the phosphorylation site in peptide substrates of G protein-coupled receptor kinase 2 (GRK2)

AU - Asai, Daisuke

AU - Murata, Masaharu

AU - Toita, Riki

AU - Kawano, Takahito

AU - Nakashima, Hideki

AU - Kang, Jeong Hun

PY - 2016/12/1

Y1 - 2016/12/1

N2 - A series of amino acid substitutions was made in a previously identified β-tubulin-derived GRK2 substrate peptide (404DEMEFTEAESNMN416) to examine the role of amino acid residues surrounding the phosphorylation site. Anionic amino acid residues surrounding the phosphorylation site played an important role in the affinity for GRK2. Compared to the original peptide, a modified peptide (Ac-EEMEFSEAEANMN-NH2) exhibited markedly higher affinity for GRK2, but very low affinity for GRK5, suggesting that it can be a sensitive and selective peptide for GRK2.

AB - A series of amino acid substitutions was made in a previously identified β-tubulin-derived GRK2 substrate peptide (404DEMEFTEAESNMN416) to examine the role of amino acid residues surrounding the phosphorylation site. Anionic amino acid residues surrounding the phosphorylation site played an important role in the affinity for GRK2. Compared to the original peptide, a modified peptide (Ac-EEMEFSEAEANMN-NH2) exhibited markedly higher affinity for GRK2, but very low affinity for GRK5, suggesting that it can be a sensitive and selective peptide for GRK2.

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