2jwn
From Proteopedia
Solution NMR structure of the protease-resistent domain of Xenopus laevis ePABP2
Structural highlights
FunctionEPA2B_XENLA Binds the poly(A) tail of mRNA. Unable to interact with the cap-binding complex and is therefore unlikely to be involved in translation initiation.[1] [UniProtKB:Q804A5] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe identified a functional domain (XlePABP2-TRP) of Xenopus laevis embryonic type II poly(A)-binding protein (XlePABP2). The NMR structure of XlePABP2-TRP revealed that the protein is a homodimer formed by the antiparallel association of beta-strands from the single RNA recognition motif (RRM) domain of each subunit. In each subunit of the homodimer, the canonical RNA recognition site is occluded by a polyproline motif. Upon poly(A) binding, XlePABP2-TRP undergoes a dimer-monomer transition that removes the polyproline motif from the RNA recognition site and allows it to be replaced by the adenosine nucleotides of poly(A). Our results provide high-resolution structural information concerning type II PABPs and an example of a single RRM domain protein that transitions from a homodimer to a monomer upon RNA binding. These findings advance our understanding of RRM domain regulation, poly(A) recognition, and are relevant to understanding how type II PABPs function in mRNA processing and human disease. Structural basis for RNA recognition by a type II poly(A)-binding protein.,Song J, McGivern JV, Nichols KW, Markley JL, Sheets MD Proc Natl Acad Sci U S A. 2008 Oct 7;105(40):15317-22. Epub 2008 Sep 29. PMID:18824697[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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