Premium
Crystal structure of the human heterogeneous ribonucleoprotein A18 RNA‐recognition motif
Author(s) -
Coburn Katherine,
Melville Zephan,
Aligholizadeh Ehson,
Roth Braden M.,
Varney Kristen M.,
Carrier France,
Pozharski Edwin,
Weber David J.
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x17003454
Subject(s) - ribonucleoprotein , heterogeneous nuclear ribonucleoprotein , antiparallel (mathematics) , rna , heterogeneous ribonucleoprotein particle , chemistry , messenger rna , microbiology and biotechnology , biology , cancer research , biochemistry , gene , physics , quantum mechanics , magnetic field
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 β‐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.