Structure of protein kinase CK2: dimerization of the human beta-subunit.

B Boldyreff, U Mietens, O G Issinger

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 1996-Jan-29
OriginalsprogEngelsk
TidsskriftFEBS Letters
Vol/bind379
Udgave nummer2
Sider (fra-til)153-6
Antal sider3
ISSN0014-5793
DOI
StatusUdgivet - 29. jan. 1996

Fingeraftryk

Casein Kinase II
Dimerization
Amino Acids
Protein-Serine-Threonine Kinases
Oncogene Proteins
Hybrid systems
Tumors
Catalytic Domain
Neoplasms

Citer dette

Boldyreff, B ; Mietens, U ; Issinger, O G. / Structure of protein kinase CK2: dimerization of the human beta-subunit. I: FEBS Letters. 1996 ; Bind 379, Nr. 2. s. 153-6.
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title = "Structure of protein kinase CK2: dimerization of the human beta-subunit.",
abstract = "Protein kinase CK2 has been shown to be elevated in all so far investigated solid tumors and its catalytic subunit has been shown to serve as an oncogene product. CK2 is a heterotetrameric serine-threonine kinase composed of two catalytic (alpha and/or alpha') and two regulatory beta-subunits. Using the two-hybrid system we could show that the alpha- or alpha'-subunits of CK2 can interact with the beta-subunits of CK2, but not with other alpha- or alpha'-subunits. By comparison, the beta-subunit of CK2 can interact with another beta-subunit. Important amino acids for successful dimerization of the beta-subunit were localized between amino acid residues 156 and 165. Furthermore, we identified residues between amino acid 170 and 180 which antagonize the dimerization.",
keywords = "Binding Sites, Casein Kinase II, Cloning, Molecular, DNA-Binding Proteins, Fungal Proteins, Humans, Macromolecular Substances, Models, Structural, Mutagenesis, Protein-Serine-Threonine Kinases, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Deletion, Transcription Factors, beta-Galactosidase",
author = "B Boldyreff and U Mietens and Issinger, {O G}",
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language = "English",
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Structure of protein kinase CK2: dimerization of the human beta-subunit. / Boldyreff, B; Mietens, U; Issinger, O G.

I: FEBS Letters, Bind 379, Nr. 2, 29.01.1996, s. 153-6.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Structure of protein kinase CK2: dimerization of the human beta-subunit.

AU - Boldyreff, B

AU - Mietens, U

AU - Issinger, O G

PY - 1996/1/29

Y1 - 1996/1/29

N2 - Protein kinase CK2 has been shown to be elevated in all so far investigated solid tumors and its catalytic subunit has been shown to serve as an oncogene product. CK2 is a heterotetrameric serine-threonine kinase composed of two catalytic (alpha and/or alpha') and two regulatory beta-subunits. Using the two-hybrid system we could show that the alpha- or alpha'-subunits of CK2 can interact with the beta-subunits of CK2, but not with other alpha- or alpha'-subunits. By comparison, the beta-subunit of CK2 can interact with another beta-subunit. Important amino acids for successful dimerization of the beta-subunit were localized between amino acid residues 156 and 165. Furthermore, we identified residues between amino acid 170 and 180 which antagonize the dimerization.

AB - Protein kinase CK2 has been shown to be elevated in all so far investigated solid tumors and its catalytic subunit has been shown to serve as an oncogene product. CK2 is a heterotetrameric serine-threonine kinase composed of two catalytic (alpha and/or alpha') and two regulatory beta-subunits. Using the two-hybrid system we could show that the alpha- or alpha'-subunits of CK2 can interact with the beta-subunits of CK2, but not with other alpha- or alpha'-subunits. By comparison, the beta-subunit of CK2 can interact with another beta-subunit. Important amino acids for successful dimerization of the beta-subunit were localized between amino acid residues 156 and 165. Furthermore, we identified residues between amino acid 170 and 180 which antagonize the dimerization.

KW - Binding Sites

KW - Casein Kinase II

KW - Cloning, Molecular

KW - DNA-Binding Proteins

KW - Fungal Proteins

KW - Humans

KW - Macromolecular Substances

KW - Models, Structural

KW - Mutagenesis

KW - Protein-Serine-Threonine Kinases

KW - Recombinant Fusion Proteins

KW - Saccharomyces cerevisiae

KW - Saccharomyces cerevisiae Proteins

KW - Sequence Deletion

KW - Transcription Factors

KW - beta-Galactosidase

U2 - 10.1016/0014-5793(95)01497-7

DO - 10.1016/0014-5793(95)01497-7

M3 - Journal article

VL - 379

SP - 153

EP - 156

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 2

ER -