Versatile retargeting of SH3 domain binding by modification of non-conserved loop residues
| Autor: | Marita Hiipakka, Kalle Saksela |
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| Jazyk: | angličtina |
| Předmět: |
Models
Molecular Phage display animal structures CD3 Complex Protein domain Biophysics Oncogene Proteins v-mos Computational biology macromolecular substances Protein Serine-Threonine Kinases Biology Signal transduction Models Biological Biochemistry environment and public health Gene Products nef Protein Structure Secondary SH3 domain Domain (software engineering) src Homology Domains Structural Biology Genetics Amino Acid Sequence Molecular Biology Conserved Sequence Immunoassay Binding Sites Membrane Proteins Cell Biology Protein engineering Ligand (biochemistry) ADAM Proteins Protein Transport SH3 p21-Activated Kinases Retargeting SOS1 Protein Protein Binding Binding domain |
| Zdroj: | FEBS Letters. (9):1735-1741 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2007.03.044 |
| Popis: | Src-homology (SH3) domain belongs to a class of ubiquitous modular protein domains found in nature. SH3 domains have a conserved surface that recognises proline-rich peptides in ligand proteins, but additional contacts also contribute to binding. Using the SH3 domain of hematopoietic cell kinase as a test case, we show that SH3 binding properties can be profoundly altered by modifications within a hexapeptide sequence in the RT-loop region that is not involved in recognition of currently known consensus SH3 target peptides. These results highlight the role of non-conserved regions in SH3 target selection, and introduce a strategy that may be generally feasible for generating artificial SH3 domains with desired ligand binding properties. |
| Databáze: | OpenAIRE |
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