5kux: Difference between revisions

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-'''Unreleased structure'''
-The entry 5kux is ON HOLD  until Paper Publication
+==Designed influenza hemagglutinin binding protein HSB.2==
+<StructureSection load='5kux' size='340' side='right' caption='[[5kux]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5kux]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KUX FirstGlance]. <br>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kuy|5kuy]]</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=5kux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kux OCA], [http://pdbe.org/5kux PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kux RCSB], [http://www.ebi.ac.uk/pdbsum/5kux PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kux ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Many viral surface glycoproteins and cell surface receptors are homo-oligomers, and thus can potentially be targeted by geometrically matched homo-oligomers that engage all subunits simultaneously to attain high avidity and/or lock subunits together. The adaptive immune system cannot generally employ this strategy since the individual antibody binding sites are not arranged with appropriate geometry to simultaneously engage multiple sites in a single target homo-oligomer. We describe a general strategy for the computational design of homo-oligomeric protein assemblies with binding functionality precisely matched to homo-oligomeric target sites. In the first step, a small protein is designed that binds a single site on the target. In the second step, the designed protein is assembled into a homo-oligomer such that the designed binding sites are aligned with the target sites. We use this approach to design high-avidity trimeric proteins that bind influenza A hemagglutinin (HA) at its conserved receptor binding site. The designed trimers can both capture and detect HA in a paper-based diagnostic format, neutralizes influenza in cell culture, and completely protects mice when given as a single dose 24 h before or after challenge with influenza.
-Authors:
+Computational design of trimeric influenza-neutralizing proteins targeting the hemagglutinin receptor binding site.,Strauch EM, Bernard SM, La D, Bohn AJ, Lee PS, Anderson CE, Nieusma T, Holstein CA, Garcia NK, Hooper KA, Ravichandran R, Nelson JW, Sheffler W, Bloom JD, Lee KK, Ward AB, Yager P, Fuller DH, Wilson IA, Baker D Nat Biotechnol. 2017 Jul;35(7):667-671. doi: 10.1038/nbt.3907. Epub 2017 Jun 12. PMID:28604661<ref>PMID:28604661</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5kux" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bernard, S M]]
+[[Category: Lee, P S]]
+[[Category: Wilson, I A]]
+[[Category: Cystatin]]
+[[Category: Designed protein]]
+[[Category: Influenza]]
+[[Category: Inhibitor]]
+[[Category: Protein binding]]