The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold

doi:10.1186/1471-2105-4-64

BMC Bioinformatics

Volume 4

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Bork P

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Research article

The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold

Francesca D Ciccarelli¹^,2 , Elisa Izaurralde¹ and Peer Bork¹^,2

¹European Molecular Biology Laboratory, Meyerhofstr. 1, 69012 Heidelberg, Germany

²Max-Delbrueck-Centrum, PO Box 740238, D-13092 Berlin, Germany

author email corresponding author email

BMC Bioinformatics 2003, 4:64doi:10.1186/1471-2105-4-64


Published:	19 December 2003

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.