Mapping the site of interaction between annexin VI and the p120GAPC2 domain
| Autor: | Andrew Chow, Debra J Gawler |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
GTPase-activating protein
Recombinant Fusion Proteins GTPase activating protein Biophysics Annexin Binding Competitive Biochemistry Cell Line Structural Biology Escherichia coli Genetics Animals Humans Annexin A6 Binding site Molecular Biology C2 domain Binding Sites Conserved region 2 Chemistry Serine Endopeptidases p120 GTPase Activating Protein Cell Biology Precipitin Tests Fusion protein Peptide Fragments Rats Ca2+ Electroporation Phospholipid Binding Linker Annexin A2 Protein Binding Ras |
| Zdroj: | FEBS Letters. 460:166-172 |
| ISSN: | 0014-5793 |
| Popis: | Annexin VI is a Ca2+-dependent membrane and phospholipid binding protein. It mediates a protein-protein interaction with the Ras p21 regulatory protein p120GAP. In this study we have mapped the binding site of GAP within the annexin VI protein. Using Far Western overlay binding assays and cell lysate competition studies we have mapped the site of interaction to the inter-lobe linker region; amino acids 325–363. Finally, using a GST fusion protein corresponding to this linker region we have demonstrated that cellular loading of the fusion protein into Rat-1 fibroblasts by electroporation blocks the interaction and co-immunoprecipitation of annexin VI and GAP. |
| Databáze: | OpenAIRE |
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