4r7d: Difference between revisions

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<StructureSection load='4r7d' size='340' side='right'caption='[[4r7d]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
<StructureSection load='4r7d' size='340' side='right'caption='[[4r7d]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[4r7d]] is a 16 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=4R7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.753&#8491;</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4r7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r7d OCA], [https://pdbe.org/4r7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r7d RCSB], [https://www.ebi.ac.uk/pdbsum/4r7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r7d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0M3KKW6_HUMAN A0A0M3KKW6_HUMAN]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Depoisier, J F]]
[[Category: Depoisier JF]]
[[Category: Didelot, G]]
[[Category: Didelot G]]
[[Category: Fischer, N]]
[[Category: Fischer N]]
[[Category: Kosco-Vilbois, M]]
[[Category: Kosco-Vilbois M]]
[[Category: Loyau, J]]
[[Category: Loyau J]]
[[Category: Magistrelli, G]]
[[Category: Magistrelli G]]
[[Category: Malinge, P]]
[[Category: Malinge P]]
[[Category: Ravn, U]]
[[Category: Ravn U]]
[[Category: Rousseau, F]]
[[Category: Rousseau F]]
[[Category: Thore, S]]
[[Category: Thore S]]
[[Category: Immune system]]
[[Category: Tlr4 antibody]]

Latest revision as of 06:30, 21 November 2024

Fab Hu 15C1Fab Hu 15C1

Structural highlights

4r7d is a 16 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 2.753Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A0M3KKW6_HUMAN

Publication Abstract from PubMed

Hu 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

  1. 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. Robust Antibody-Antigen Complexes Prediction Generated by Combining Sequence Analyses, Mutagenesis, In Vitro Evolution, X-ray Crystallography and In Silico Docking. J Mol Biol. 2015 May 24. pii: S0022-2836(15)00300-9. doi:, 10.1016/j.jmb.2015.05.016. PMID:26013163 doi:http://dx.doi.org/10.1016/j.jmb.2015.05.016

4r7d, resolution 2.75Å

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