1au1: Difference between revisions
New page: left|200px<br /> <applet load="1au1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1au1, resolution 2.2Å" /> '''HUMAN INTERFERON-BET... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1au1.gif|left|200px]]<br /> | [[Image:1au1.gif|left|200px]]<br /><applet load="1au1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1au1" size=" | |||
caption="1au1, resolution 2.2Å" /> | caption="1au1, resolution 2.2Å" /> | ||
'''HUMAN INTERFERON-BETA CRYSTAL STRUCTURE'''<br /> | '''HUMAN INTERFERON-BETA CRYSTAL STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
Type I interferons (IFNs) are helical cytokines that have diverse | 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== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
1AU1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1AU1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AU1 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 26: | Line 25: | ||
[[Category: interferon]] | [[Category: interferon]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:17 2008'' | ||
Revision as of 12:48, 21 February 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.
DiseaseDisease
Known diseases associated with this structure: Kaposi sarcoma, susceptibility to OMIM:[147620], Osteopenia/osteoporosis OMIM:[147620]
About this StructureAbout this Structure
1AU1 is a Single protein structure of sequence from Homo sapiens with as ligand. 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 Thu Feb 21 11:48:17 2008