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Article

Structural analysis of interdomain mobility in ribosomal L1 proteins.

Acta crystallographica. Section D, Biological crystallography - 1 Dec 2011

Tishchenko S, Nikonova E, Kostareva O, Gabdulkhakov A, Piendl W, Nevskaya N, Garber M, Nikonov S

Abstract excerpt

Ribosomal protein L1 consists of two domains connected by two oppositely directed fragments of the polypeptide chain in a hinge-resembling fashion. The domain arrangement determines the overall shape of the protein, corresponding to an open or a closed conformation. Ribosomal L1 proteins from archaea demonstrate the open conformation in both isolated and RNA-bound forms. RNA-free ribosomal L1 proteins from...

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PMID: 22120739
DOI: 10.1107/S0907444911043435

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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