5opy: Difference between revisions

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'''Unreleased structure'''


The entry 5opy is ON HOLD  until Paper Publication
==Crystal structure of anti-alphaVbeta3 integrin Fab LM609==
<StructureSection load='5opy' size='340' side='right' caption='[[5opy]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5opy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OPY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OPY FirstGlance]. <br>
</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=5opy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5opy OCA], [http://pdbe.org/5opy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5opy RCSB], [http://www.ebi.ac.uk/pdbsum/5opy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5opy ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The LM609 antibody specifically recognizes alphaVbeta3 integrin and inhibits angiogenesis, bone resorption, and viral infections in an arginine-glycine-aspartate-independent manner. LM609 entered phase II clinical trials for the treatment of several cancers and was also used for alphaVbeta3-targeted radioimmunotherapy. To elucidate the mechanisms of recognition and inhibition of alphaVbeta3 integrin, we solved the structure of the LM609 antigen-binding fragment by X-ray crystallography and determined its binding affinity for alphaVbeta3. Using single-particle electron microscopy, we show that LM609 binds at the interface between the beta-propeller domain of the alphaV chain and the betaI domain of the beta3 chain, near the RGD-binding site, of all observed integrin conformational states. Integrating these data with fluorescence size-exclusion chromatography, we demonstrate that LM609 sterically hinders access of large ligands to the RGD-binding pocket, without obstructing it. This work provides a structural framework to expedite future efforts utilizing LM609 as a diagnostic or therapeutic tool.


Authors: Backovic, M., Veesler, D., Borst, A.J., James, Z.M., Zagotta, W., Ginsberg, M., Rey, F.A., DiMaio, F.
The Therapeutic Antibody LM609 Selectively Inhibits Ligand Binding to Human alphaVbeta3 Integrin via Steric Hindrance.,Borst AJ, James ZM, Zagotta WN, Ginsberg M, Rey FA, DiMaio F, Backovic M, Veesler D Structure. 2017 Oct 7. pii: S0969-2126(17)30298-8. doi:, 10.1016/j.str.2017.09.007. PMID:29033288<ref>PMID:29033288</ref>


Description: Crystal structure of anti-alphaVbeta3 integrin Fab LM609
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Zagotta, W]]
<div class="pdbe-citations 5opy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Backovic, M]]
[[Category: Backovic, M]]
[[Category: Borst, A J]]
[[Category: DiMaio, F]]
[[Category: Ginsberg, M]]
[[Category: James, Z M]]
[[Category: Rey, F A]]
[[Category: Veesler, D]]
[[Category: Veesler, D]]
[[Category: James, Z.M]]
[[Category: Zagotta, W]]
[[Category: Ginsberg, M]]
[[Category: Antigen-binding fragment]]
[[Category: Borst, A.J]]
[[Category: Fab]]
[[Category: Rey, F.A]]
[[Category: Immune system]]
[[Category: Dimaio, F]]
[[Category: Lm609]]
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