1G9L

SOLUTION STRUCTURE OF THE PABC DOMAIN OF HUMAN POLY(A) BINDING PROTEIN

Summary for 1G9L

• Entry DOI: 10.2210/pdb1g9l/pdb
• NMR Information: BMRB: 4915
• Descriptor: POLYADENYLATE-BINDING PROTEIN 1 (1 entity in total)
• Functional Keywords: all-helical domain, rna binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 15286.45

Authors

Kozlov, G.,Trempe, J.-F.,Khaleghpour, K.,Kahvejian, A.,Ekiel, I.,Gehring, K. (deposition date: 2000-11-24, release date: 2001-03-14, Last modification date: 2024-05-22)

Primary citation

Kozlov, G.,Trempe, J.F.,Khaleghpour, K.,Kahvejian, A.,Ekiel, I.,Gehring, K.
Structure and function of the C-terminal PABC domain of human poly(A)-binding protein.
Proc.Natl.Acad.Sci.USA, 98:4409-4413, 2001

PubMed Abstract: We have determined the solution structure of the C-terminal quarter of human poly(A)-binding protein (hPABP). The protein fragment contains a protein domain, PABC [for poly(A)-binding protein C-terminal domain], which is also found associated with the HECT family of ubiquitin ligases. By using peptides derived from PABP interacting protein (Paip) 1, Paip2, and eRF3, we show that PABC functions as a peptide binding domain. We use chemical shift perturbation analysis to identify the peptide binding site in PABC and the major elements involved in peptide recognition. From comparative sequence analysis of PABC-binding peptides, we formulate a preliminary PABC consensus sequence and identify human ataxin-2, the protein responsible for type 2 spinocerebellar ataxia (SCA2), as a potential PABC ligand.

PubMed: 11287632
DOI: 10.1073/pnas.071024998

Experimental method

SOLUTION NMR