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The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold
Francesca D Ciccarelli1, Elisa Izaurralde, Peer Bork
1European Molecular Biology Laboratory, Meyerhofstr, 1, 69012 Heidelberg, Germany. francesca.ciccarelli@embl.de
BMC Bioinformatics
|December 23, 2003
Summary
Researchers discovered a new protein module, the PAM domain, found in key cellular complexes. This domain likely mediates interactions with other proteins, aiding complex assembly and function.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Multimeric protein complexes are crucial for cellular pathways.
- Understanding protein domain organization reveals functional roles.
- Interconnectedness of protein complexes highlights the need for detailed characterization.
Purpose of the Study:
- To identify and characterize novel protein domains within multimeric complexes.
- To elucidate the structural and functional significance of newly identified domains.
Main Methods:
- Bioinformatic analysis to identify conserved protein modules.
- Structural prediction of identified domains.
- Comparative analysis of domain occurrence in known protein complexes.
Main Results:
- Identification of the PAM (PCI/PINT associated module) domain.
- The PAM domain is approximately 200 residues long with a predicted TPR-like alpha-helical fold.
- The PAM domain is present in subunits of well-characterized complexes like the 26S proteasome and COP-9 signalosome.
Conclusions:
- The PAM domain's presence in specific subunits suggests a role in protein-protein interactions.
- Its predicted all-alpha-helical fold supports a function in mediating transient binding.
- This finding contributes to understanding the modular organization of multimeric protein complexes.