5tbx: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CIRBP_HUMAN CIRBP_HUMAN]] Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Acts as a translational activator. Seems to play an essential role in cold-induced suppression of cell proliferation. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN. Acts as a translational repressor (By similarity). Promotes assembly of stress granules (SGs), when overexpressed.<ref>PMID:11574538</ref> <ref>PMID:16513844</ref> | [[http://www.uniprot.org/uniprot/CIRBP_HUMAN CIRBP_HUMAN]] Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Acts as a translational activator. Seems to play an essential role in cold-induced suppression of cell proliferation. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN. Acts as a translational repressor (By similarity). Promotes assembly of stress granules (SGs), when overexpressed.<ref>PMID:11574538</ref> <ref>PMID:16513844</ref> | ||
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== Publication Abstract from PubMed == | |||
The heterogeneous ribonucleoprotein A18 (hnRNP A18) is upregulated in hypoxic regions of various solid tumors and promotes tumor growth via the coordination of mRNA transcripts associated with pro-survival genes. Thus, hnRNP A18 represents an important therapeutic target in tumor cells. Presented here is the first X-ray crystal structure to be reported for the RNA-recognition motif of hnRNP A18. By comparing this structure with those of homologous RNA-binding proteins (i.e. hnRNP A1), three residues on one face of an antiparallel beta-sheet (Arg48, Phe50 and Phe52) and one residue in an unstructured loop (Arg41) were identified as likely to be involved in protein-nucleic acid interactions. This structure helps to serve as a foundation for biophysical studies of this RNA-binding protein and structure-based drug-design efforts for targeting hnRNP A18 in cancer, such as malignant melanoma, where hnRNP A18 levels are elevated and contribute to disease progression. | |||
Crystal structure of the human heterogeneous ribonucleoprotein A18 RNA-recognition motif.,Coburn K, Melville Z, Aligholizadeh E, Roth BM, Varney KM, Carrier F, Pozharski E, Weber DJ Acta Crystallogr F Struct Biol Commun. 2017 Apr 1;73(Pt 4):209-214. doi:, 10.1107/S2053230X17003454. Epub 2017 Mar 22. PMID:28368279<ref>PMID:28368279</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | == References == | ||
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