Is TALL-1 a trimer or a virus-like cluster?

Eugene A. Zhukovsky (), Jie-Oh Lee, Michael Villegas, Cheryl Chan, Seung Chu and Cameron Mroske
Additional contact information
Eugene A. Zhukovsky: Xencor
Jie-Oh Lee: KAIST
Michael Villegas: Xencor
Cheryl Chan: Xencor
Seung Chu: Xencor
Cameron Mroske: Xencor

Nature, 2004, vol. 427, issue 6973, 413-414

Abstract: Abstract Native TALL-1 (B-cell activation factor, BAFF; also known as BlyS) was initially described as a homotrimer1,2,3, but Liu and colleagues claim that it is a 60-subunit complex4,5,6 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 virus4,5,6. 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.

Date: 2004
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DOI: 10.1038/427413a

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