4r7d: Difference between revisions
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==Fab Hu 15C1== | ==Fab Hu 15C1== | ||
<StructureSection load='4r7d' size='340' side='right' caption='[[4r7d]], [[Resolution|resolution]] 2.75Å' scene=''> | <StructureSection load='4r7d' size='340' side='right'caption='[[4r7d]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4r7d]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R7D FirstGlance]. <br> | <table><tr><td colspan='2'>[[4r7d]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R7D FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r7n|4r7n]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r7n|4r7n]]</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=4r7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r7d RCSB], [http://www.ebi.ac.uk/pdbsum/4r7d 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=4r7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r7d OCA], [http://pdbe.org/4r7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r7d RCSB], [http://www.ebi.ac.uk/pdbsum/4r7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r7d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4r7d" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Depoisier, J F]] | [[Category: Depoisier, J F]] | ||
[[Category: Didelot, G]] | [[Category: Didelot, G]] | ||
Revision as of 12:58, 1 May 2019
Fab Hu 15C1Fab Hu 15C1
Structural highlights
Publication Abstract from PubMedHu 15C1 is a potent anti-human Toll-like receptor 4 (TLR4) neutralizing antibody. To better understand the molecular basis of its biological activity, we used a multidisciplinary approach to generate an accurate model of the Hu 15C1-TLR4 complex. By combining site-directed mutagenesis, in vitro antibody evolution, affinity measurements and X-ray crystallography of Fab fragments, we identified key interactions across the Hu 15C1-TLR4 interface. These contact points were used as restraints to predict the structure of the Fab region of Hu 15C1 bound to TLR4 using computational molecular docking. This model was further evaluated and validated by additional site-directed mutagenesis studies. The predicted structure of the Hu 15C1-TLR4 complex indicates that the antibody antagonizes the receptor dimerization necessary for its activation. This study exemplifies how iterative cycles of antibody engineering can facilitate the discovery of components of antibody-target interactions. Robust Antibody-Antigen Complexes Prediction Generated by Combining Sequence Analyses, Mutagenesis, In Vitro Evolution, X-ray Crystallography and In Silico Docking.,Loyau J, Didelot G, Malinge P, Ravn U, Magistrelli G, Depoisier JF, Pontini G, Poitevin Y, Kosco-Vilbois M, Fischer N, Thore S, Rousseau F J Mol Biol. 2015 May 24. pii: S0022-2836(15)00300-9. doi:, 10.1016/j.jmb.2015.05.016. PMID:26013163[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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