1au1
From Proteopedia
|
HUMAN INTERFERON-BETA CRYSTAL STRUCTURE
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Kaposi sarcoma, susceptibility to OMIM:[147620], Osteopenia/osteoporosis OMIM:[147620]
About this Structure
1AU1 is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of human interferon beta at 2.2-A resolution., Karpusas M, Nolte M, Benton CB, Meier W, Lipscomb WN, Goelz S, Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11813-8. PMID:9342320
Page seeded by OCA on Mon Nov 12 16:01:49 2007
