3q0q
From Proteopedia
Crystal structure of the PUMILIO-homology domain from Human PUMILIO2 in complex with p38alpha NREa
Structural highlights
FunctionPUM2_HUMAN Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. Its interactions and tissue specificity suggest that it may be required to support proliferation and self-renewal of stem cells by regulating the translation of key transcripts. Publication Abstract from PubMedHuman 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 p38alpha 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. Alternate modes of cognate RNA recognition by human PUMILIO proteins.,Lu G, Hall TM Structure. 2011 Mar 9;19(3):361-7. PMID:21397187[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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