PROSITE documentation PDOC51309Poly(A)-binding protein C-terminal (PABC) domain profile
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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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Kozlov G. Trempe J.-F. Khaleghpour K. Kahvejian A. Ekiel I. Gehring K. |
| Title | Structure and function of the C-terminal PABC domain of human poly(A)-binding protein. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 98:4409-4413(2001). | |
| PubMed ID | 11287632 | |
| DOI | 10.1073/pnas.071024998 |
| 2 | Authors | Kozlov G. Siddiqui N. Coillet-Matillon S. Trempe J.-F. Ekiel I. Sprules T. Gehring K. |
| Title | Solution structure of the orphan PABC domain from Saccharomyces cerevisiae poly(A)-binding protein. | |
| Source | J. Biol. Chem. 277:22822-22828(2002). | |
| PubMed ID | 11940585 | |
| DOI | 10.1074/jbc.M201230200 |
| 3 | Authors | Siddiqui N. Kozlov G. D'Orso I. Trempe J.-F. Gehring K. |
| Title | Solution structure of the C-terminal domain from poly(A)-binding protein in Trypanosoma cruzi: a vegetal PABC domain. | |
| Source | Protein Sci. 12:1925-1933(2003). | |
| PubMed ID | 12930992 |
| 4 | Authors | Kozlov 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. |
| Title | Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase. | |
| Source | EMBO J. 23:272-281(2004). | |
| PubMed ID | 14685257 | |
| DOI | 10.1038/sj.emboj.7600048 |
| 5 | Authors | Siddiqui N. Osborne M.J. Gallie D.R. Gehring K. |
| Title | Solution Structure of the PABC Domain from Wheat Poly (A)-Binding Protein: An Insight into RNA Metabolic and Translational Control in Plants. | |
| Source | Biochemistry 46:4221-4231(2007). | |
| PubMed ID | 17358048 | |
| DOI | 10.1021/bi061986d |
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