Unknown

Dataset Information

0

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


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.

SUBMITTER: Karpusas M 

PROVIDER: S-EPMC23607 | biostudies-literature | 1997 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Karpusas M M   Nolte M M   Benton C B CB   Meier W W   Lipscomb W N WN   Goelz S S  

Proceedings of the National Academy of Sciences of the United States of America 19971001 22


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  ...[more]

Similar Datasets

| S-EPMC45116 | biostudies-other
| S-EPMC4794786 | biostudies-literature
| S-EPMC5786005 | biostudies-literature
| S-EPMC6512338 | biostudies-literature
| EMPIAR-10061 | biostudies-other
| S-EPMC4548775 | biostudies-literature
| S-EPMC3606563 | biostudies-literature
| S-EPMC3795567 | biostudies-literature
| S-EPMC2929978 | biostudies-literature