5fv2: Difference between revisions
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The | ==Crystal structure of hVEGF in complex with VH domain antibody== | ||
<StructureSection load='5fv2' size='340' side='right'caption='[[5fv2]], [[Resolution|resolution]] 3.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fv2]] is a 6 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=5FV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FV2 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]] 3.45Å</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=5fv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fv2 OCA], [https://pdbe.org/5fv2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fv2 RCSB], [https://www.ebi.ac.uk/pdbsum/5fv2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fv2 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A potent VEGF inhibitor with novel antibody architecture and antigen binding mode has been developed. The molecule, hereafter referred to as VEGF dual dAba (domain antibody), was evaluated in vitro for binding to VEGF and for potency in VEGF driven models and compared with other anti-VEGF biologics that have been used in ocular anti-angiogenic therapeutic regimes. VEGF dual dAb is more potent than bevacizumab and ranibizumab for VEGF binding and inhibition of VEGF RBAb (receptor binding assay) formats and when compared using in vitro models of angiogenesis; and displays comparable inhibition to aflibercept, (Eylea). VEGF dual dAb is dimeric and each monomer contains two distinct anti-VEGF domain antibodies attached via linkers to a human IgG1 Fc domain. Mechanistically, the enhanced in vitro potency of VEGF dual dAb in comparison to other anti-VEGF biologics can be explained by increased binding stoichiometry. A consistent model of the target engagement has been built based on the X-ray complexes of each of the two isolated domain antibodies with the VEGF antigen. | |||
Novel interaction mechanism of a domain antibody based inhibitor of human vascular endothelial growth factor with greater potency than ranibizumab and bevacizumab and improved capacity over aflibercept.,Walker A, Chung CW, Neu M, Burman M, Batuwangala T, Jones G, Tang CM, Steward M, Mullin M, Tournier N, Lewis A, Korczynska J, Chung V, Catchpole I J Biol Chem. 2016 Jan 4. pii: jbc.M115.691162. PMID:26728464<ref>PMID:26728464</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Batuwangala | <div class="pdbe-citations 5fv2" style="background-color:#fffaf0;"></div> | ||
[[Category: Chung | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[VEGF 3D Structures|VEGF 3D Structures]] | |||
*[[3D structures of human antibody|3D structures of human antibody]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Batuwangala T]] | |||
[[Category: Chung C]] | |||
Latest revision as of 07:07, 21 November 2024
Crystal structure of hVEGF in complex with VH domain antibodyCrystal structure of hVEGF in complex with VH domain antibody
Structural highlights
Publication Abstract from PubMedA potent VEGF inhibitor with novel antibody architecture and antigen binding mode has been developed. The molecule, hereafter referred to as VEGF dual dAba (domain antibody), was evaluated in vitro for binding to VEGF and for potency in VEGF driven models and compared with other anti-VEGF biologics that have been used in ocular anti-angiogenic therapeutic regimes. VEGF dual dAb is more potent than bevacizumab and ranibizumab for VEGF binding and inhibition of VEGF RBAb (receptor binding assay) formats and when compared using in vitro models of angiogenesis; and displays comparable inhibition to aflibercept, (Eylea). VEGF dual dAb is dimeric and each monomer contains two distinct anti-VEGF domain antibodies attached via linkers to a human IgG1 Fc domain. Mechanistically, the enhanced in vitro potency of VEGF dual dAb in comparison to other anti-VEGF biologics can be explained by increased binding stoichiometry. A consistent model of the target engagement has been built based on the X-ray complexes of each of the two isolated domain antibodies with the VEGF antigen. Novel interaction mechanism of a domain antibody based inhibitor of human vascular endothelial growth factor with greater potency than ranibizumab and bevacizumab and improved capacity over aflibercept.,Walker A, Chung CW, Neu M, Burman M, Batuwangala T, Jones G, Tang CM, Steward M, Mullin M, Tournier N, Lewis A, Korczynska J, Chung V, Catchpole I J Biol Chem. 2016 Jan 4. pii: jbc.M115.691162. PMID:26728464[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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