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FEBS Letters
Volume 211, Issue 2 p. 179-184
Research letters
Free Access

Tumour necrosis factor is a compact trimer

Paul Wingfield, 

Paul Wingfield

Biogen S.A. 3 route de Troinex, F-1227 Carouge, Geneva, Switzerland

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Roger H. Pain, 

Corresponding Author

Roger H. Pain

Biogen S.A. 3 route de Troinex, F-1227 Carouge, Geneva, Switzerland

Department of Biochemistry, University of Newcastle, Newcastle upon Tyne, NE1 7RU, England

Correspondence address: R.H. Pain, Dept of Bio-chemistry, University of Newcastle, Newcastle upon Tyne, NE1 7RU, England.Search for more papers by this author
Stewart Craig, 

Stewart Craig

Biogen S.A. 3 route de Troinex, F-1227 Carouge, Geneva, Switzerland

Department of Biochemistry, University of Newcastle, Newcastle upon Tyne, NE1 7RU, England

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First published: January 26, 1987
https://doi.org/10.1016/0014-5793(87)81432-1
Citations: 110

Abstract

Recombinant produced human tumour necrosis factor (TNF) has been studied to characterise the subunit structure of the protein. TNF is shown to be a trimer M r 52000 in which the subunits are associated in a compact, triangular form. In secondary structure it belongs to the all-β class of proteins. It has high thermodynamic stability and the unfolded subunits can fold and associate spontaneously to form native, biologically active TNF.