3hc3: Difference between revisions
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<StructureSection load='3hc3' size='340' side='right'caption='[[3hc3]], [[Resolution|resolution]] 1.72Å' scene=''> | <StructureSection load='3hc3' size='340' side='right'caption='[[3hc3]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3hc3]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3hc3]] is a 2 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=3HC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HC3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hc3 OCA], [https://pdbe.org/3hc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hc3 RCSB], [https://www.ebi.ac.uk/pdbsum/3hc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hc3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arndt | [[Category: Arndt JW]] | ||
[[Category: Jordan | [[Category: Jordan JL]] | ||
[[Category: Lugovskoy | [[Category: Lugovskoy A]] | ||
[[Category: Wang | [[Category: Wang D]] | ||
Revision as of 10:19, 6 September 2023
BHA10 IgG1 Fab double mutant variant - antibody directed at human LTBRBHA10 IgG1 Fab double mutant variant - antibody directed at human LTBR
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBispecific immunoglobulin-like antibodies capable of engaging multiple antigens represent a promising new class of therapeutic agents. Engineering of these molecules requires optimization of the molecular properties of one of the domain components. Here, we present a detailed crystallographic and computational characterization of the stabilization patterns in the lymphotoxin-beta receptor (LTbetaR) binding Fv domain of an anti-LTbetaR/anti-TNF-related apoptosis inducing ligand receptor-2 (TRAIL-R2) bispecific immunoglobulin-like antibody. We further describe a new hierarchical structure-guided approach toward engineering of antibody-like molecules to enhance their thermal and chemical stability. Proteins 2009. (c) 2009 Wiley-Liss, Inc. Structural understanding of stabilization patterns in engineered bispecific Ig-like antibody molecules.,Jordan JL, Arndt JW, Hanf K, Li G, Hall J, Demarest S, Huang F, Wu X, Miller B, Glaser S, Fernandez EJ, Wang D, Lugovskoy A Proteins. 2009 Jun 19. PMID:19626705[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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