Multiple sclerosis: Difference between revisions

Revision as of 18:19, 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 . It consists of five , as well as multiple interconnecting . Helices A, B and D run , and helices C and E run to the other three helices, but 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

^[5]

Interferon receptor bound to interferon alpha

A comparison of Interferon Alpha to Interferon Beta

Synchronize the applets showing Interferons Alpha and Beta by clicking the checkbox

Click on the green links to the left to see key structural features of Interferon Beta (PDB entry 1ifa)

Drag the structure with the mouse to rotate

Other TreatmentsOther Treatments

CopaxoneCopaxone

ReferencesReferences

↑ 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
↑ http://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

Relevant 3D StructuresRelevant 3D Structures

Interferon BetaInterferon Beta

1au1 - Homo sapiens

1ifa, 1wu3 - Mus musculus

Interferon ReceptorsInterferon Receptors

3s98, 3se3, 3se4, 1n6u, 1n6v, 2hym, 2kz1, 2lag, 3s8w, 3s9d - Homo sapiens

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Kirsten Eldredge

[Biochem_Text-1] Voet, D., Voet, J.G., and C. Pratt. Fundamentals of Biochemistry 3rd Edition. Hoboken, NJ: John Wiley and Sons, 2008. Print.

[Structure-2] 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

[UniProt-3] ttp://www.uniprot.org/uniprot/P00784

[4] [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

[Interferon_Receptor_Structure-5] 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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[2]

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[5]

@@ Line 25: / Line 25: @@
 {|
-|<applet load='1itf.pdb' name='A' size='250' frame='true' align='right' caption='Interferon Alpha' align='left' scene='Multiple_sclerosis/Ifna_take_2/5'/>
+|<applet load='1itf.pdb' name='A' size='250' frame='true' align='right' caption='Interferon Alpha' align='left' scene='Multiple_sclerosis/Ifna_take_3/1'/>
 |<applet load='1ifa.pdb' name='B' size='250' frame='true' align='right' caption='Interferon Beta' align='left' scene='Multiple_sclerosis/Interferon_beta/8'/>
 |}