title: The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold.
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.
authors.affiliation: European Molecular Biology Laboratory, Meyerhofstr, 1, 69012 Heidelberg, Germany. francesca.ciccarelli@embl.de
authors.forename: Francesca D
authors.initials: FD
authors.lastname: Ciccarelli
authors.forename: Elisa
authors.initials: E
authors.lastname: Izaurralde
authors.forename: Peer
authors.initials: P
authors.lastname: Bork
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000852:Anopheles / Q000737:chemistry; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000502:physiology; D000075686:COP9 Signalosome Complex; D018797:Cell Cycle Proteins / Q000737:chemistry / Q000502:physiology; D016384:Consensus Sequence; D029721:Drosophila Proteins / Q000737:chemistry / Q000502:physiology; D018257:Helix-Loop-Helix Motifs / Q000502:physiology; D006801:Humans; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000502:physiology; D046912:Multiprotein Complexes; D009492:Neurospora crassa / Q000737:chemistry; D009687:Nuclear Proteins; D010447:Peptide Hydrolases / Q000737:chemistry / Q000502:physiology; D010802:Phylogeny; D046988:Proteasome Endopeptidase Complex; D011494:Protein Kinases / Q000737:chemistry / Q000502:physiology; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000502:physiology; D012097:Repressor Proteins / Q000737:chemistry / Q000502:physiology; D012261:Ribonucleoproteins / Q000737:chemistry / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000502:physiology; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry / Q000502:physiology; D016415:Sequence Alignment / Q000379:methods
chemical_list: D029681:Arabidopsis Proteins; C474638:CSN2 protein, Arabidopsis; D018797:Cell Cycle Proteins; D029721:Drosophila Proteins; D046911:Macromolecular Substances; D009097:Multienzyme Complexes; D046912:Multiprotein Complexes; D009687:Nuclear Proteins; C403291:RPN3 protein, S cerevisiae; D012097:Repressor Proteins; D012261:Ribonucleoproteins; D029701:Saccharomyces cerevisiae Proteins; D029702:Schizosaccharomyces pombe Proteins; C476348:Thp1 protein, S cerevisiae; D011494:Protein Kinases; C120564:Sac3 protein kinase; D017346:Protein Serine-Threonine Kinases; D010447:Peptide Hydrolases; D000075686:COP9 Signalosome Complex; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease