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TNF ligands: is TALL-1 a trimer or a virus-like cluster?

Identifieur interne : 000261 ( Ncbi/Merge ); précédent : 000260; suivant : 000262

TNF ligands: is TALL-1 a trimer or a virus-like cluster?

Auteurs : Eugene A. Zhukovsky [États-Unis] ; Jie-Oh Lee ; Michael Villegas ; Cheryl Chan ; Seung Chu ; Cameron Mroske

Source :

RBID : pubmed:14749821

Descripteurs français

English descriptors

Abstract

Native TALL-1 (B-cell activation factor, BAFF; also known as BlyS) was initially described as a homotrimer, but Liu and colleagues claim that it is a 60-subunit complex on the basis of their results from X-ray crystallography and size-exclusion chromatography. They consider TALL-1 60-mers to be the biologically active form, and the arrangement of the 60-mers resembles that of the capsid of satellite tobacco necrosis virus. Here we show that active TALL-1 is trimeric under normal physiological conditions and that formation of higher-order oligomers is an artefact of tagging the amino terminus of the protein with a histidine tag.

DOI: 10.1038/427413a
PubMed: 14749821

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pubmed:14749821

Le document en format XML

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<div type="abstract" xml:lang="en">Native TALL-1 (B-cell activation factor, BAFF; also known as BlyS) was initially described as a homotrimer, but Liu and colleagues claim that it is a 60-subunit complex on the basis of their results from X-ray crystallography and size-exclusion chromatography. They consider TALL-1 60-mers to be the biologically active form, and the arrangement of the 60-mers resembles that of the capsid of satellite tobacco necrosis virus. Here we show that active TALL-1 is trimeric under normal physiological conditions and that formation of higher-order oligomers is an artefact of tagging the amino terminus of the protein with a histidine tag.</div>
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