1au1
From Proteopedia
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| - | [[Image:1au1.gif|left|200px]] | + | [[Image:1au1.gif|left|200px]] |
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| - | '''HUMAN INTERFERON-BETA CRYSTAL STRUCTURE''' | + | {{Structure |
| + | |PDB= 1au1 |SIZE=350|CAPTION= <scene name='initialview01'>1au1</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN INTERFERON-BETA CRYSTAL STRUCTURE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AU1 is a [ | + | 1AU1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AU1 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9342320 9342320] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: interferon]] | [[Category: interferon]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:16 2008'' |
Revision as of 08:02, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 10:02:16 2008
