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| [[Image:1au1.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1au1| PDB=1au1 | SCENE= }} | | {{STRUCTURE_1au1| PDB=1au1 | SCENE= }} |
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| '''HUMAN INTERFERON-BETA CRYSTAL STRUCTURE'''
| | ===HUMAN INTERFERON-BETA CRYSTAL STRUCTURE=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_9342320}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9342320 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9342320}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Immune system]] | | [[Category: Immune system]] |
| [[Category: Interferon]] | | [[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 Mon Jun 30 17:35:28 2008'' |