1owx
From Proteopedia
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'''Solution structure of the C-terminal RRM of human La (La225-334)''' | '''Solution structure of the C-terminal RRM of human La (La225-334)''' | ||
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[[Category: Kelly, G.]] | [[Category: Kelly, G.]] | ||
[[Category: Manolaridis, I.]] | [[Category: Manolaridis, I.]] | ||
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Revision as of 01:22, 3 May 2008
Solution structure of the C-terminal RRM of human La (La225-334)
Overview
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.
About this Structure
1OWX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element., Jacks A, Babon J, Kelly G, Manolaridis I, Cary PD, Curry S, Conte MR, Structure. 2003 Jul;11(7):833-43. PMID:12842046 Page seeded by OCA on Sat May 3 04:22:50 2008
Categories: Homo sapiens | Single protein | Babon, J. | Cary, P D. | Conte, M R. | Curry, S. | Jacks, A. | Kelly, G. | Manolaridis, I. | Rrm