3KTR

Structural basis of ataxin-2 recognition by poly(A)-binding protein

Summary for 3KTR

• Entry DOI: 10.2210/pdb3ktr/pdb
• Related: 3KTP
• Descriptor: Polyadenylate-binding protein 1, Ataxin-2, CADMIUM ION, ... (5 entities in total)
• Functional Keywords: protein-protein complex, acetylation, alternative splicing, cytoplasm, methylation, mrna processing, mrna splicing, nucleus, phosphoprotein, rna-binding, spliceosome, neurodegeneration, parkinsonism, polymorphism, spinocerebellar ataxia, triplet repeat expansion, protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P11940; Cytoplasm (By similarity): Q99700
• Total number of polymer chains: 2
• Total formula weight: 11665.54

Authors

Kozlov, G.,Gehring, K. (deposition date: 2009-11-25, release date: 2010-02-23, Last modification date: 2023-09-06)

Primary citation

Kozlov, G.,Safaee, N.,Rosenauer, A.,Gehring, K.
Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein.
J.Biol.Chem., 285:13599-13606, 2010

PubMed Abstract: Poly(A)-binding protein (PABPC1) is involved in multiple aspects of mRNA processing and translation. It is a component of RNA stress granules and binds the RNA-induced silencing complex to promote degradation of silenced mRNAs. Here, we report the crystal structures of the C-terminal Mlle (or PABC) domain in complex with peptides from GW182 (TNRC6C) and Ataxin-2. The structures reveal overlapping binding sites but with unexpected diversity in the peptide conformation and residues involved in binding. The mutagenesis and binding studies show low to submicromolar binding affinity with overlapping but distinct specificity determinants. These results rationalize the role of the Mlle domain of PABPC1 in microRNA-mediated mRNA deadenylation and suggest a more general function in the assembly of cytoplasmic RNA granules.

PubMed: 20181956
DOI: 10.1074/jbc.M109.089540

Experimental method

X-RAY DIFFRACTION (1.7 Å)