NDLI: The crystal structure of human interferon beta at 2.2-A resolution.

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The crystal structure of human interferon beta at 2.2-A resolution.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Nolte, M. Lipscomb, W. N. Goelz, S. Karpusas, M. Benton, C. B. Meier, W.
Description	Author Affiliation: Karpusas M ( Biogen, Inc., 12 Cambridge Center, Cambridge, MA 02142, USA. Michael_Karpusas@biogen.com);
Abstract	Type I interferons (IFNs) are helical cytokines that have diverse biological activities despite the fact that they appear to interact with the same receptor system. To achieve a better understanding of the structural basis for the different activities of alpha and beta IFNs, we have determined the crystal structure of glycosylated human IFN-beta at 2.2-A resolution by molecular replacement. The molecule adopts a fold similar to that of the previously determined structures of murine IFN-beta and human IFN-alpha2b but displays several distinct structural features. Like human IFN-alpha2b, human IFN-beta contains a zinc-binding site at the interface of the two molecules in the asymmetric unit, raising the question of functional relevance for IFN-beta dimers. However, unlike the human IFN-alpha2b dimer, in which homologous surfaces form the interface, human IFN-beta dimerizes with contact surfaces from opposite sides of the molecule. The relevance of the structure to the effects of point mutations in IFN-beta at specific exposed residues is discussed. A potential role of ligand-ligand interactions in the conformational assembly of IFN receptor components is discussed.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	22
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Glycoproteins Chemistry Interferon-beta Computer Simulation Crystallography, X-Ray DNA Mutational Analysis Dimerization Interferons Models, Molecular Molecular Sequence Data Mutagenesis Protein Conformation Comparative Study Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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