4ypg: Difference between revisions

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-'''Unreleased structure'''
-The entry 4ypg is ON HOLD
+==Structural Insights Into the Neutralization Properties of a Human Anti-Interferon Monoclonal Antibody==
+<StructureSection load='4ypg' size='340' side='right'caption='[[4ypg]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4ypg]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YPG FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ypg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ypg OCA], [https://pdbe.org/4ypg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ypg RCSB], [https://www.ebi.ac.uk/pdbsum/4ypg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ypg ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q6PJF2_HUMAN Q6PJF2_HUMAN]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We report the three-dimensional structure of human interferon alpha-2A (IFN-alpha2A) bound to the Fab fragment of a therapeutic monoclonal antibody (sifalimumab; IgG1/k). The structure of the corresponding complex was solved at a resolution of 3.0 A using molecular replacement and constitutes the first reported structure of a human type I IFN bound to a therapeutic antibody. This study revealed the major contribution made by the first complementarity determining region (CDR) in each of sifalimumab light and heavy chains. These data also provided the molecular basis for sifalimumab mechanism of action. We propose that its interferon-neutralizing properties are the results of direct competition for IFN-alpha2A binding to the IFN receptor subunit 1 (IFNAR1) and do not involve inhibiting IFN-alpha2A binding to the IFN receptor subunit 2 (IFNAR2).
-Authors: Vaheh Oganesyan, William F. DallAcqua
+Structural Insights Into the Neutralization Properties of the Fully Human, Anti-Interferon Monoclonal Antibody Sifalimumab.,Oganesyan V, Peng L, Woods RM, Wu H, Dall'Acqua WF J Biol Chem. 2015 Apr 29. pii: jbc.M115.652156. PMID:25925951<ref>PMID:25925951</ref>
-Description: Structural Insights Into the Neutralization Properties of a Human Anti-Interferon Monoclonal Antibody
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Vaheh Oganesyan, William F. Dallacqua]]
+<div class="pdbe-citations 4ypg" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Interferon 3D structures|Interferon 3D structures]]
+*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Dall'Acqua WF]]
+[[Category: Oganesyan V]]