3hc3: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: '''Unreleased structure''' The entry 3hc3 is ON HOLD Authors: Arndt, J.W., Jordan, J. L., Lugovskoy, A., Wang, D. Description: BHA10 IgG1 Fab double mutant variant -antibody directed a...
 
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 3hc3 is ON HOLD
==BHA10 IgG1 Fab double mutant variant - antibody directed at human LTBR==
<StructureSection load='3hc3' size='340' side='right'caption='[[3hc3]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</td></tr>
<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'>[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hc/3hc3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hc3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


Authors: Arndt, J.W., Jordan, J. L., Lugovskoy, A., Wang, D.
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<ref>PMID:19626705</ref>


Description: BHA10 IgG1 Fab double mutant variant -antibody directed at human LTBR
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3hc3" style="background-color:#fffaf0;"></div>


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 13 09:37:54 2009''
==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Sandbox 20009|Sandbox 20009]]
*[[3D structures of human antibody|3D structures of human antibody]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arndt JW]]
[[Category: Jordan JL]]
[[Category: Lugovskoy A]]
[[Category: Wang D]]

Latest revision as of 08:52, 17 October 2024

BHA10 IgG1 Fab double mutant variant - antibody directed at human LTBRBHA10 IgG1 Fab double mutant variant - antibody directed at human LTBR

Structural highlights

3hc3 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.72Å
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

3hc3, resolution 1.72Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA