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PROSITE documentation PDOC51309 [for PROSITE entry PS51309]

Poly(A)-binding protein C-terminal (PABC) domain profile





Description

The ~75-residue poly(A)-binding protein C-terminal domain (PABC) is a peptide-binding domain found in:

  • poly(A)-binding proteins (PABPs), ubiquitous RNA binding proteins found in all eukaryotes. They are implicated in stabilizing mRNA and promoting translation. PABPs are modular proteins consisting of an N-terminal region with four RNA recognition motifs (RRMs) (see <PDOC00030>) and a PABC domain.
  • The HYD (for hyperplastic discs), EDD or Rat100 family of ubiquitin E3 protein ligases. HYD ubiquitin ligases contain a HECT domain (see <PDOC50237>).

The PABC domain binds a conserved motif of 12-15 amino acids, termed PABP-interacting motif (PAM)-2, with conserved alanine, phenylalanine and proline residues at position 7, 10 and 12 [1,2,3,4,5].

The PABC domain consists of five (see <PDB:1JH4; A>) or four (see <PDB:1IFW; A>) α-helices that form a compact structure with a well packed hydrophobic core. Characteristic to all PABC domains, the last four helices fold into a right-handed super coil. They encompass the peptide-binding site and among PABC domains, sequences conservation is highest among helices 2, 3, and 5, which are required for peptide recognition [1,2,3,4,5]. A phylogenetic analysis of the PABC domain reveals that they can be categorized into three main classes: animal, vegetal and a 'divergent' group including Saccharomyces cerevisiae, Schizosaccharomyces pombe, and the HYD family of ubiquitin ligases [2,3].

The profile we developed covers the entire PABC domain.

Last update:

April 2007 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

PABC, PS51309; Poly(A)-binding protein C-terminal (PABC) domain profile  (MATRIX)


References

1AuthorsKozlov G. Trempe J.-F. Khaleghpour K. Kahvejian A. Ekiel I. Gehring K.
TitleStructure and function of the C-terminal PABC domain of human poly(A)-binding protein.
SourceProc. Natl. Acad. Sci. U.S.A. 98:4409-4413(2001).
PubMed ID11287632
DOI10.1073/pnas.071024998

2AuthorsKozlov G. Siddiqui N. Coillet-Matillon S. Trempe J.-F. Ekiel I. Sprules T. Gehring K.
TitleSolution structure of the orphan PABC domain from Saccharomyces cerevisiae poly(A)-binding protein.
SourceJ. Biol. Chem. 277:22822-22828(2002).
PubMed ID11940585
DOI10.1074/jbc.M201230200

3AuthorsSiddiqui N. Kozlov G. D'Orso I. Trempe J.-F. Gehring K.
TitleSolution structure of the C-terminal domain from poly(A)-binding protein in Trypanosoma cruzi: a vegetal PABC domain.
SourceProtein Sci. 12:1925-1933(2003).
PubMed ID12930992

4AuthorsKozlov G. De Crescenzo G. Lim N.S. Siddiqui N. Fantus D. Kahvejian A. Trempe J.-F. Elias D. Ekiel I. Sonenberg N. O'Connor-McCourt M. Gehring K.
TitleStructural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase.
SourceEMBO J. 23:272-281(2004).
PubMed ID14685257
DOI10.1038/sj.emboj.7600048

5AuthorsSiddiqui N. Osborne M.J. Gallie D.R. Gehring K.
TitleSolution Structure of the PABC Domain from Wheat Poly (A)-Binding Protein: An Insight into RNA Metabolic and Translational Control in Plants.
SourceBiochemistry 46:4221-4231(2007).
PubMed ID17358048
DOI10.1021/bi061986d



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