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| |<applet load='1itf.pdb' name='A' size='250' frame='true' align='right' caption='Interferon Alpha' align='left' scene='Multiple_sclerosis/Ifna_take_3/3'/> | | |<applet load='1itf.pdb' name='A' size='250' frame='true' align='right' caption='Interferon Alpha' align='left' scene='Multiple_sclerosis/Ifna_take_3/4'/> |
| |<applet load='1ifa.pdb' name='B' size='250' frame='true' align='right' caption='Interferon Beta' align='left' scene='Multiple_sclerosis/Ifnb_take_2/1'/> | | |<applet load='1ifa.pdb' name='B' size='250' frame='true' align='right' caption='Interferon Beta' align='left' scene='Multiple_sclerosis/Ifnb_take_2/2'/> |
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Revision as of 15:43, 10 April 2012
Please have patience as I edit this page over the next few weeks! Thank you!--Kirsten Eldredge 04:22, 9 April 2012 (IDT)
| Interferon-β
Interferon-β is a protein growth factor that stimulates an antiviral defense. Its encoding gene is one of only two known vertebrate structural genes that lacks introns.[1]
Interferon-β is a relatively simple biological response modifier, with several identifiable regions. It consists of five alpha helices, as well as multiple interconnecting loop regions. Helices A, B and D run parallel to one another, and helices C and E run anti-parallel to the other three helices, but parallel to one another. Helix A consists of residues 6-23; Helix B consists of residues 49-65; Helix C consists of residues 77-91; Helix D consists of residues 112-131; and Helix E consists of residues 135-155.[2][3]
Interferons alpha and beta interact with a receptor at the surface of [4]
Interferon receptor
Interferon receptor domains
N-domain, with two disulfide bonds,
C-domain, with one disulfide bond
linker region
termini regions, no structure.
eight clashes between domains[5]
Interferon receptor bound to interferon alpha
Interferon alpha
A comparison of Interferon Alpha to Interferon Beta
Synchronize the applets showing Interferons Alpha and Beta by clicking the checkbox
- ↑ Voet, D., Voet, J.G., and C. Pratt. Fundamentals of Biochemistry 3rd Edition. Hoboken, NJ: John Wiley and Sons, 2008. Print.
- ↑ Kudo M. Management of hepatocellular carcinoma: from prevention to molecular targeted therapy. Oncology. 2010 Jul;78 Suppl 1:1-6. Epub 2010 Jul 8. PMID:20616576 doi:10.1159/000315222
- ↑ https://www.uniprot.org/uniprot/P00784
- ↑ [1] Samuel, C.E. "Interferons, Interferon Receptors, Signal Transducer and Transcriptional Activators, and Inteferon Regulatory Factors." J Biol Chem 2007 282: 20045-20046. First Published on May 14, 2007, doi:10.1074/jbc.R700025200
- ↑ Chill JH, Quadt SR, Levy R, Schreiber G, Anglister J. The human type I interferon receptor: NMR structure reveals the molecular basis of ligand binding. Structure. 2003 Jul;11(7):791-802. PMID:12842042
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Other Treatments
Copaxone
References
Relevant 3D Structures
Interferon Beta
1au1 - Homo sapiens
1ifa, 1wu3 - Mus musculus
Interferon Receptors
3s98, 3se3, 3se4, 1n6u, 1n6v, 2hym, 2kz1, 2lag, 3s8w, 3s9d - Homo sapiens
