1au1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1au1.gif|left|200px]] | [[Image:1au1.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1au1", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_1au1| PDB=1au1 | SCENE= }} | |||
}} | |||
'''HUMAN INTERFERON-BETA CRYSTAL STRUCTURE''' | '''HUMAN INTERFERON-BETA CRYSTAL STRUCTURE''' | ||
| Line 28: | Line 25: | ||
[[Category: Lipscomb, W.]] | [[Category: Lipscomb, W.]] | ||
[[Category: Nolte, M.]] | [[Category: Nolte, M.]] | ||
[[Category: | [[Category: Cytokine]] | ||
[[Category: | [[Category: Helical cytokine]] | ||
[[Category: | [[Category: Immune system]] | ||
[[Category: | [[Category: Interferon]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:41:24 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 10:41, 2 May 2008
HUMAN INTERFERON-BETA CRYSTAL STRUCTURE
OverviewOverview
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.
About this StructureAbout this Structure
1AU1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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 Fri May 2 10:41:24 2008