The TPR2B Domain of the Hsp70/Hsp90 Organizing Protein (Hop) May Contribute Towards Its Dimerization
Autor: | Sheril Daniel, Victoria M. Longshaw, Gregory L. Blatch, Linda L. Stephens |
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Rok vydání: | 2009 |
Předmět: |
Molecular Sequence Data
Proteins Sequence alignment General Medicine Biology Biochemistry Hsp90 Protein Structure Tertiary Hsp70 Hop (networking) Protein structure Structural Biology Domain (ring theory) Biophysics biology.protein Amino Acid Sequence Protein Multimerization Site-directed mutagenesis Dimerization Sequence Alignment Peptide sequence Heat-Shock Proteins |
Zdroj: | Protein & Peptide Letters. 16:402-407 |
ISSN: | 0929-8665 |
Popis: | The role of the TPR2B domain of Hop is as yet unknown. We have shown here by site directed mutagenesis and size exclusion chromatography for the first time that the TPR1 and TPR2B domains of Hop independently dimerized, and that the dimerization of TPR2B was not dependent on its predicted two-carboxylate clamp residues. Furthermore, our data indicated that the dimerization of Hop and its domains was not disrupted in the presence of Hsp70 and Hsp90 peptides. |
Databáze: | OpenAIRE |
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