FEBS letters, 2001-09, Vol.505 (1), p.42-46
2001
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Details
- Autor(en) / Beteiligte
- Titel
- The carboxy-terminal domain of Grp94 binds to protein kinase CK2α but not to CK2 holoenzyme
- Ist Teil von
- FEBS letters, 2001-09, Vol.505 (1), p.42-46
- Ort / Verlag
- England: Elsevier B.V
- Erscheinungsjahr
- 2001
- Quelle
- Wiley-Blackwell Journals
- Beschreibungen/Notizen
- Surface plasmon resonance analysis shows that the carboxy-terminal domain of Grp94 (Grp94-CT, residues 518–803) physically interacts with the catalytic subunit of protein kinase CK2 (CK2α) under non-stressed conditions. A K D of 4×10 −7 was determined for this binding. Heparin competed with Grp94-CT for binding to CK2α. CK2β also inhibited the binding of Grp94-CT to CK2α, and CK2 holoenzyme reconstituted in vitro was unable to bind Grp94-CT. The use of CK2α mutants made it possible to map the Grp94-CT binding site to the four lysine stretch (residues 74–77) present in helix C of CK2α. Grp94-CT stimulated the activity of CK2α wild-type but was ineffective on the CK2α K74–77A mutant.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0014-5793eISSN: 1873-3468DOI: 10.1016/S0014-5793(01)02781-8Titel-ID: cdi_proquest_miscellaneous_71171884
- Format
- –
- Schlagworte
- Amino Acid Sequence, Binding Sites, Casein Kinase II, Catalytic Domain, CK2, protein kinase CK2 (formerly casein kinase 2 or II), Grp94, Grp94, glucose-regulated protein of 94 kDa (also known as gp96, endoplasmin or hsp100), HSP70 Heat-Shock Proteins - genetics, HSP70 Heat-Shock Proteins - metabolism, hsp90, heat shock protein of 90 kDa, Humans, Lysine, Membrane Proteins - genetics, Membrane Proteins - metabolism, Molecular chaperone, Molecular Sequence Data, Mutation, Peptides - metabolism, Protein kinase CK2, Protein Subunits, Protein-Serine-Threonine Kinases - metabolism, SPR, surface plasmon resonance, Substrate Specificity, Surface Plasmon Resonance, wt, wild-type