6cvk: Difference between revisions

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-'''Unreleased structure'''
-The entry 6cvk is ON HOLD  until Paper Publication
+==Hepatitis B e-antigen in complex with scFv e13==
+<StructureSection load='6cvk' size='340' side='right' caption='[[6cvk]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6cvk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CVK FirstGlance]. <br>
+</td></tr><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=6cvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cvk OCA], [http://pdbe.org/6cvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cvk RCSB], [http://www.ebi.ac.uk/pdbsum/6cvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cvk ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Hepatitis B virus (HBV) is the leading cause of liver disease worldwide. While an adequate vaccine is available, current treatment options are limited, not highly effective, and associated with adverse effects, encouraging the development of alternative therapeutics. The HBV core gene encodes two different proteins: core, which forms the viral nucleocapsid, and pre-core, which serves as an immune modulator with multiple points of action. The two proteins mostly have the same sequence, although they differ at their N and C termini and in their dimeric arrangements. Previously, we engineered two human-framework antibody fragments (Fab/scFv) with nano- to picomolar affinities for both proteins. Here, by means of X-ray crystallography, analytical ultracentrifugation, and electron microscopy, we demonstrate that the antibodies have non-overlapping epitopes and effectively block biologically important assemblies of both proteins. These properties, together with the anticipated high tolerability and long half-lives of the antibodies, make them promising therapeutics.
-Authors: Eren, E., Steven, A.C., Wingfield, P.T.
+Structures of Hepatitis B Virus Core- and e-Antigen Immune Complexes Suggest Multi-point Inhibition.,Eren E, Watts NR, Dearborn AD, Palmer IW, Kaufman JD, Steven AC, Wingfield PT Structure. 2018 Jul 17. pii: S0969-2126(18)30244-2. doi:, 10.1016/j.str.2018.06.012. PMID:30100358<ref>PMID:30100358</ref>
-Description: Hepatitis B e-antigen in complex with scFv e13
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Steven, A.C]]
+<div class="pdbe-citations 6cvk" style="background-color:#fffaf0;"></div>
-[[Category: Wingfield, P.T]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Eren, E]]
+[[Category: Steven, A C]]
+[[Category: Wingfield, P T]]
+[[Category: E-antigen]]
+[[Category: Hepatitis b]]
+[[Category: Single chain variable fragment]]
+[[Category: Viral protein]]
+[[Category: Viral protein-immune system complex]]