4iml: Difference between revisions

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'''Unreleased structure'''


The entry 4iml is ON HOLD  until Paper Publication
==CrossFab binding to human Angiopoietin 2==
<StructureSection load='4iml' size='340' side='right'caption='[[4iml]], [[Resolution|resolution]] 2.93&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4iml]] is a 4 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=4IML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IML 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]] 2.931&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4iml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iml OCA], [https://pdbe.org/4iml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iml RCSB], [https://www.ebi.ac.uk/pdbsum/4iml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iml ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bispecific antibodies are considered as a promising class of future biotherapeutic molecules. They comprise binding specificities for two different antigens, which may provide additive or synergistic modes of action. There is a wide variety of design alternatives for such bispecific antibodies, including the "CrossMab" format. CrossMabs contain a domain crossover in one of the antigen-binding (Fab) parts, together with the "knobs-and-holes" approach, to enforce the correct assembly of four different polypeptide chains into an IgG-like bispecific antibody. We determined the crystal structure of a hAng-2-binding Fab in its crossed and uncrossed form and show that CH1-CL-domain crossover does not induce significant perturbations of the structure and has no detectable influence on target binding.


Authors: Fenn, S., Schiller, C., Griese, J., Hopfner, K.-P., Kettenberger, H.
Crystal structure of an anti-Ang2 CrossFab demonstrates complete structural and functional integrity of the variable domain.,Fenn S, Schiller CB, Griese JJ, Duerr H, Imhof-Jung S, Gassner C, Moelleken J, Regula JT, Schaefer W, Thomas M, Klein C, Hopfner KP, Kettenberger H PLoS One. 2013 Apr 17;8(4):e61953. doi: 10.1371/journal.pone.0061953. Print 2013. PMID:23613981<ref>PMID:23613981</ref>


Description: CrossFab binding to human Angiopoietin 2
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4iml" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Fenn S]]
[[Category: Griese J]]
[[Category: Hopfner K-P]]
[[Category: Kettenberger H]]
[[Category: Schiller C]]
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