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4z5r

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'''Unreleased structure'''
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==Rontalizumab Fab bound to Interferon-a2==
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<StructureSection load='4z5r' size='340' side='right' caption='[[4z5r]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4z5r]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z5R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z5R FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4z5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z5r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4z5r RCSB], [http://www.ebi.ac.uk/pdbsum/4z5r PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/IFNA2_HUMAN IFNA2_HUMAN]] Produced by macrophages, IFN-alpha have antiviral activities.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Interferons-alpha (IFN-alpha) are the expressed gene products comprising thirteen type I interferons with protein pairwise sequence similarities in the 77-96% range. Three other widely expressed human type I interferons, IFN-beta, IFN-kappa and IFN-omega have sequences 29-33%, 29-32% and 56-60% similar to the IFN-alphas, respectively. Type I interferons act on immune cells by producing subtly different immune-modulatory effects upon binding to the extracellular domains of a heterodimeric cell surface receptor composed of IFNAR1 and IFNAR2, most notably anti-viral effects. IFN-alpha has been used to treat infection by hepatitis-virus type C (HCV) and a correlation between hyperactivity of IFN-alpha -induced signaling and systemic lupus erythematosis (SLE), or lupus, has been noted. Anti-IFN-alpha antibodies including rontalizumab have been under clinical study for the treatment of lupus. To better understand the rontalizumab mechanism of action and specificity, we determined the X-ray crystal structure of the Fab fragment of rontalizumab bound to human IFN-alpha2 at 3A resolution and find substantial overlap of the antibody and IFNA2 epitopes on IFN-alpha2. This article is protected by copyright. All rights reserved.
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The entry 4z5r is ON HOLD until Paper Publication
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Structural Basis of the Broadly Neutralizing anti-Interferon-alpha Antibody Rontalizumab.,Maurer B, Bosanac I, Shia S, Kwong M, Corpuz R, Vandlen R, Schmidt K, Eigenbrot C Protein Sci. 2015 Jun 22. doi: 10.1002/pro.2729. PMID:26099203<ref>PMID:26099203</ref>
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Authors: Eigenbrot, C., Maurer, B., Bosanac, I.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description:
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bosanac, I]]
[[Category: Bosanac, I]]
[[Category: Eigenbrot, C]]
[[Category: Eigenbrot, C]]
[[Category: Maurer, B]]
[[Category: Maurer, B]]
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[[Category: Antibody]]
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[[Category: Cytokine-immune system complex]]
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[[Category: Interferon]]

Revision as of 14:43, 8 July 2015

Rontalizumab Fab bound to Interferon-a2

4z5r, resolution 3.00Å

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