Dataset Information
The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold.
Ontology highlight
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.
SUBMITTER: Ciccarelli FD
PROVIDER: S-EPMC319699 | biostudies-literature | 2003 Dec
REPOSITORIES: biostudies-literature
Publications
The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold.
BMC bioinformatics 20031219
<h4>Background</h4>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.<h4>Results</h4>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 ...[more]