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| Item Type: | Article |
|---|---|
| Title: | The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold |
| Creators Name: | Ciccarelli, F.D. and Izaurralde, E. and Bork, P. |
| Abstract: | BACKGROUND: Multimeric protein complexes have a role in many cellular pathways and are highly interconnected with various other proteins. The characterization of their domain composition and organization provides useful information on the specific role of each region of their sequence. RESULTS: We identified a new module, the PAM domain (PCI/PINT associated module), present in single subunits of well characterized multiprotein complexes, like the regulatory lid of the 26S proteasome, the COP-9 signalosome and the Sac3-Thp1 complex. This module is an around 200 residue long domain with a predicted TPR-like all-alpha-helical fold. CONCLUSIONS: The occurrence of the PAM domain in specific subunits of multimeric protein complexes, together with the role of other all-alpha-helical folds in protein-protein interactions, suggest a function for this domain in mediating transient binding to diverse target proteins. |
| Keywords: | Amino Acid Sequence, Anopheles, Arabidopsis Proteins, Cell Cycle Proteins, Consensus Sequence, Drosophila Proteins, Helix-Loop-Helix Motifs, Macromolecular Substances, Molecular Sequence Data, Multienzyme Complexes, Multiprotein Complexes, Neurospora crassa, Nuclear Proteins, Peptide Hydrolases, Phylogeny, Proteasome Endopeptidase Complex, Protein Kinases, Protein-Serine-Threonine Kinases, Repressor Proteins, Ribonucleoproteins, Saccharomyces cerevisiae Proteins, Schizosaccharomyces pombe Proteins, Sequence Alignment, Animals |
| Source: | BMC Bioinformatics |
| ISSN: | 1471-2105 |
| Publisher: | BioMed Central |
| Volume: | 4 |
| Page Range: | 64 |
| Date: | 19 December 2003 |
| Official Publication: | https://doi.org/10.1186/1471-2105-4-64 |
| PubMed: | View item in PubMed |
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