3hc0: Difference between revisions

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==BHA10 IgG1 wild-type Fab - antibody directed at human LTBR==
==BHA10 IgG1 wild-type Fab - antibody directed at human LTBR==
<StructureSection load='3hc0' size='340' side='right' caption='[[3hc0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3hc0' size='340' side='right' caption='[[3hc0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hc3|3hc3]], [[3hc4|3hc4]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hc3|3hc3]], [[3hc4|3hc4]]</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=3hc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hc0 OCA], [http://pdbe.org/3hc0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hc0 RCSB], [http://www.ebi.ac.uk/pdbsum/3hc0 PDBsum]</span></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=3hc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hc0 OCA], [http://pdbe.org/3hc0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hc0 RCSB], [http://www.ebi.ac.uk/pdbsum/3hc0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hc0 ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hc/3hc0_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hc/3hc0_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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==See Also==
==See Also==
*[[Antibody|Antibody]]
*[[Antibody 3D structures|Antibody 3D structures]]
== References ==
== References ==
<references/>
<references/>

Revision as of 08:54, 7 December 2018

BHA10 IgG1 wild-type Fab - antibody directed at human LTBRBHA10 IgG1 wild-type Fab - antibody directed at human LTBR

Structural highlights

3hc0 is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

Bispecific 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 Also

References

  1. 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. Structural understanding of stabilization patterns in engineered bispecific Ig-like antibody molecules. Proteins. 2009 Jun 19. PMID:19626705 doi:10.1002/prot.22502

3hc0, resolution 1.90Å

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OCA