Yang, Zhiru and West, Anthony P., Jr. and Bjorkman, Pamela J. (2009) Crystal structure of TNFα complexed with a poxvirus MHC-related TNF binding protein. Nature Structural & Molecular Biology, 16 (11). pp. 1189-1191. ISSN 1545-9985 http://resolver.caltech.edu/CaltechAUTHORS:20091123-100928279
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Abstract
The poxvirus 2L protein binds tumor necrosis factor-α (TNFα) to inhibit host antiviral and immune responses. The 2.8-Å 2L–TNFα structure reveals three symmetrically arranged 2L molecules per TNFα trimer. 2L resembles class I major histocompatibility complex (MHC) molecules but lacks a peptide-binding groove and β2-microglobulin light chain. Overlap between the 2L and host TNF receptor-binding sites on TNFα rationalizes 2L inhibition of TNFα–TNF receptor interactions and prevention of TNFα-induced immune responses.
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| Additional Information: | © 2009 Nature Publishing Group, a division of Macmillan Publishers Limited. Received 29 April; accepted 26 August; published online 18 October 2009. Diffraction data were collected at the Stanford Synchrotron Radiation Laboratory. We thank the Caltech Protein Expression Center and the Gordon and Betty Moore Foundation for support of the Molecular Observatory at Caltech. This work was supported by a Life Sciences Research Foundation Fellowship (Z.Y.) and the Howard Hughes Medical Institute. Z.Y. and A.P.W. performed the experiments; Z.Y., A.P.W. and P.J.B. analyzed and interpreted that data; P.J.B. oversaw the project. | ||||||||||
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| Record Number: | CaltechAUTHORS:20091123-100928279 | ||||||||||
| Persistent URL: | http://resolver.caltech.edu/CaltechAUTHORS:20091123-100928279 | ||||||||||
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| Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. | ||||||||||
| ID Code: | 16781 | ||||||||||
| Collection: | CaltechAUTHORS | ||||||||||
| Deposited By: | Jason Perez | ||||||||||
| Deposited On: | 24 Nov 2009 19:15 | ||||||||||
| Last Modified: | 26 Dec 2012 11:34 |
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