4PLX: Crystal Structure Of The Triple-helical Stability Element At The 3' End Of Malat1

Citation:
Abstract
Metastasis-associated lung adenocarcinoma transcript 1 (MALAT1) is a highly abundant nuclear long noncoding RNA that promotes malignancy. A 3'-stem-loop structure is predicted to confer stability by engaging a downstream A-rich tract in a triple helix, similar to the expression and nuclear retention element (ENE) from the KSHV polyadenylated nuclear RNA. The 3.1-A-resolution crystal structure of the human MALAT1 ENE and A-rich tract reveals a bipartite triple helix containing stacks of five and four U*A-U triples separated by a C+*G-C triplet and C-G doublet, extended by two A-minor interactions. In vivo decay assays indicate that this blunt-ended triple helix, with the 3' nucleotide in a U*A-U triple, inhibits rapid nuclear RNA decay. Interruption of the triple helix by the C-G doublet induces a 'helical reset' that explains why triple-helical stacks longer than six do not occur in nature.
PDB ID: 4PLXDownload
MMDB ID: 121036
PDB Deposition Date: 2014/5/19
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 3.1  Å
Source Organism:
Biological Unit for 4PLX: monomeric; determined by author
Molecular Components in 4PLX
Label Count Molecule
Nucleotide(1 molecule)
1
Core ENE Hairpin and A-rich Tract From Malat1
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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