3Q0S

Crystal structure of the PUMILIO-homology domain from Human PUMILIO2 in complex with erk2 NRE

Summary for 3Q0S

• Entry DOI: 10.2210/pdb3q0s/pdb
• Related: 3Q0L 3Q0M 3Q0N 3Q0O 3Q0P 3Q0Q 3Q0R
• Descriptor: Pumilio homolog 2, 5'-R(UP*GP*UP*AP*CP*AP*UP*C)-3' (3 entities in total)
• Functional Keywords: puf, pumilio-homolgy domain, gene regulation, rna binding, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm (Probable): Q8TB72
• Total number of polymer chains: 2
• Total formula weight: 43012.24

Authors

Lu, G.,Hall, T.M.T. (deposition date: 2010-12-15, release date: 2011-03-16, Last modification date: 2013-06-19)

Primary citation

Lu, G.,Hall, T.M.
Alternate modes of cognate RNA recognition by human PUMILIO proteins.
Structure, 19:361-367, 2011

PubMed Abstract: Human PUMILIO1 (PUM1) and PUMILIO2 (PUM2) are members of the PUMILIO/FBF (PUF) family that regulate specific target mRNAs posttranscriptionally. Recent studies have identified mRNA targets associated with human PUM1 and PUM2. Here, we explore the structural basis of natural target RNA recognition by human PUF proteins through crystal structures of the RNA-binding domains of PUM1 and PUM2 in complex with four cognate RNA sequences, including sequences from p38α and erk2 MAP kinase mRNAs. We observe three distinct modes of RNA binding around the fifth RNA base, two of which are different from the prototypical 1 repeat:1 RNA base binding mode previously identified with model RNA sequences. RNA-binding affinities of PUM1 and PUM2 are not affected dramatically by the different binding modes in vitro. However, these modes of binding create structurally variable recognition surfaces that suggest a mechanism in vivo for recruitment of downstream effector proteins defined by the PUF:RNA complex.

PubMed: 21397187
DOI: 10.1016/j.str.2010.12.019

Experimental method

X-RAY DIFFRACTION (2 Å)