5TBX

hnRNP A18 RNA Recognition Motif

Summary for 5TBX

• Entry DOI: 10.2210/pdb5tbx/pdb
• Descriptor: Cold-inducible RNA-binding protein, ACETATE ION, NICKEL (II) ION, ... (4 entities in total)
• Functional Keywords: rna-binding protein, rna binding protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 20460.19

Authors

Coburn, K.M.,Melville, Z.,Aligholizadeh, E.,Roth, B.M.,Varney, K.M.,Weber, D.J. (deposition date: 2016-09-13, release date: 2017-04-12, Last modification date: 2024-04-03)

Primary citation

Coburn, K.,Melville, Z.,Aligholizadeh, E.,Roth, B.M.,Varney, K.M.,Carrier, F.,Pozharski, E.,Weber, D.J.
Crystal structure of the human heterogeneous ribonucleoprotein A18 RNA-recognition motif.
Acta Crystallogr F Struct Biol Commun, 73:209-214, 2017

PubMed Abstract: 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.

PubMed: 28368279
DOI: 10.1107/S2053230X17003454

Experimental method

X-RAY DIFFRACTION (1.767 Å)