| DOI | Resolve DOI: https://doi.org/10.1038/sj.emboj.7600048 |
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| Author | Search for: Kozlov, Guennadi; Search for: De Crescenzo, Gregory1; Search for: Lim, Nadia S; Search for: Siddiqui, Nadeem; Search for: Fantus, Daniel; Search for: Kahvejian, Avak; Search for: Trempe, Jean-Francois; Search for: Elias, Demetra; Search for: Ekiel, Irena1; Search for: Sonenberg, Nahum; Search for: O'Connor-McCourt, Maureen1; Search for: Gehring, Kalle |
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| Affiliation | - National Research Council of Canada. NRC Biotechnology Research Institute
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| Format | Text, Article |
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| Subject | genome; mutagenesis; peptides; pharmaceutical; proteins; surface plasmon resonance; tail |
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| Abstract | The C-terminal domain of poly(A)-binding protein (PABC) is a peptide-binding domain found in poly(A)-binding proteins (PABPs) and a HECT (homologous to E6 -AP C-terminus) family E3 ubiquitin ligase. In protein synthesis, the PABC domain of PABP functions to recruit several translation factors possessing the PABP-interacting motif 2 (PAM2) to the mRNA poly(A) tail. We have determined the solution structure of the human PABC domain in complex with two peptides from PABP-interacting protein-1 (Paip1) and Paip2. The structures show a novel mode of peptide recognition, in which the peptide binds as a pair of beta-turns with extensive hydrophobic, electrostatic and aromatic stacking interactions. Mutagenesis of PABC and peptide residues was used to identify key protein -peptide interactions and quantified by isothermal calorimetry, surface plasmon resonance and GST pull-down assays. The results provide insight into the specificity of PABC in mediating PABP-protein interactions |
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| Publication date | 2004 |
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| In | |
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| Note | English14685257 |
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| Language | English |
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| NRC number | 46169 |
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| NPARC number | 3539976 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 239599b9-dbcc-44b0-bb52-3aca0e979d4f |
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| Record created | 2009-03-01 |
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| Record modified | 2020-04-17 |
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