Structural basis of ligand recognition by PABC, a highly specific peptide -binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase

Download
  1. Get@NRC: Structural basis of ligand recognition by PABC, a highly specific peptide -binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1038/sj.emboj.7600048
AuthorSearch for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for:
TypeArticle
Journal titleEmbo J
Volume23
Issue2
Pages272281; # of pages: 10
Subjectgenome; Human; Mutagenesis; Peptides; pha; Proteins; Surface Plasmon Resonance; Tail
AbstractThe C-terminal domain of poly(A)-binding protein (PABC) is a peptide-binding domain found in poly(A)-binding proteins (PABPs) and a HECT (homologous to E6 -AP C-terminus) family E3 ubiquitin ligase. In protein synthesis, the PABC domain of PABP functions to recruit several translation factors possessing the PABP-interacting motif 2 (PAM2) to the mRNA poly(A) tail. We have determined the solution structure of the human PABC domain in complex with two peptides from PABP-interacting protein-1 (Paip1) and Paip2. The structures show a novel mode of peptide recognition, in which the peptide binds as a pair of beta-turns with extensive hydrophobic, electrostatic and aromatic stacking interactions. Mutagenesis of PABC and peptide residues was used to identify key protein -peptide interactions and quantified by isothermal calorimetry, surface plasmon resonance and GST pull-down assays. The results provide insight into the specificity of PABC in mediating PABP-protein interactions
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
NoteEnglish14685257
Peer reviewedNo
NRC number46169
NPARC number3539976
Export citationExport as RIS
Report a correctionReport a correction
Record identifier239599b9-dbcc-44b0-bb52-3aca0e979d4f
Record created2009-03-01
Record modified2016-05-09
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)