1OWX: Solution structure of the C-terminal RRM of human La (La225-334)

The La protein is an important component of ribonucleoprotein complexes that acts mainly as an RNA chaperone to facilitate correct processing and maturation of RNA polymerase III transcripts, but can also stimulate translation initiation. We report here the structure of the C-terminal domain of human La, which comprises an atypical RNA recognition motif (La225-334) and a long unstructured C-terminal tail. The central beta sheet of La225-334 reveals novel features: the putative RNA binding surface is formed by a five-stranded beta sheet and, strikingly, is largely obscured by a long C-terminal alpha helix that encompasses a recently identified nuclear retention element. Contrary to previous observations, we find that the La protein does not contain a dimerization domain.
PDB ID: 1OWXDownload
MMDB ID: 24328
PDB Deposition Date: 2003/3/31
Updated in MMDB: 2007/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 1OWX
Label Count Molecule
Protein (1 molecule)
Lupus LA Protein(Gene symbol: SSB)
Molecule annotation
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Citing MMDB