4ulw

From Proteopedia

Crystal structure of the ROQ-domain of human ROQUIN1

Structural highlights

4ulw is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.91Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RC3H1_HUMAN Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more mRNAs (By similarity). Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs (By similarity). In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity (By similarity). In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression (By similarity). Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation (By similarity).

Publication Abstract from PubMed

Roquin proteins mediate mRNA deadenylation by recognizing a conserved class of stem-loop RNA degradation motifs via their Roquin domain. Here we present the crystal structure of a Roquin domain, revealing a mostly helical protein fold bearing a winged helix-turn-helix motif. By combining structural, biochemical and mutation analyses, we gain insight into the mode of RNA binding. We show that the winged helix-turn-helix motif is involved in the binding of constitutive decay elements-containing stem-loop mRNAs. Moreover, we provide biochemical evidence that Roquin proteins are additionally able to bind to duplex RNA and have the potential to be functional in different oligomeric states.

Roquin binding to target mRNAs involves a winged helix-turn-helix motif.,Schuetz A, Murakawa Y, Rosenbaum E, Landthaler M, Heinemann U Nat Commun. 2014 Dec 11;5:5701. doi: 10.1038/ncomms6701. PMID:25504471^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations

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References

↑ Schuetz A, Murakawa Y, Rosenbaum E, Landthaler M, Heinemann U. Roquin binding to target mRNAs involves a winged helix-turn-helix motif. Nat Commun. 2014 Dec 11;5:5701. doi: 10.1038/ncomms6701. PMID:25504471 doi:http://dx.doi.org/10.1038/ncomms6701