6ugv: Difference between revisions

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'''Unreleased structure'''


The entry 6ugv is ON HOLD
==Crystal structure of the Fab fragment of anti-TNFa antibody infliximab (Remicade) in a I-centered orthorhombic crystal form, Lot C==
<StructureSection load='6ugv' size='340' side='right'caption='[[6ugv]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ugv]] 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=6UGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UGV 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MRY:MESO-ERYTHRITOL'>MRY</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=6ugv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ugv OCA], [https://pdbe.org/6ugv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ugv RCSB], [https://www.ebi.ac.uk/pdbsum/6ugv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ugv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6P5S8_HUMAN Q6P5S8_HUMAN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Higher-order structure (HOS) assessment is an important component of biosimilarity evaluations. While established spectroscopic methods are routinely used to characterize structure and evaluate similarity, the addition of X-ray crystallographic analysis to these biophysical methods enables orthogonal elucidation of HOS at higher resolution. METHODS: Crystal structures of the infliximab biosimilar PF-06438179/GP1111 and the reference product Remicade((R)), sourced from US and European Union markets, were determined and compared to evaluate HOS similarity. Analytical ultracentrifugation studies were conducted to understand reversible self-association. RESULTS: In contrast to more routine spectroscopic methods, the crystal structures enable three-dimensional assessment of complementarity-determining regions and other local regions at near-atomic resolution. The biosimilar structures are highly similar to those of the reference product, as demonstrated visually and though all-atom root-mean-squared deviation measurements. CONCLUSION: The structures provide new insights into the physicochemical properties of the proposed biosimilar and the reference product, further strengthening the 'totality of evidence' in the evaluation of similarity.


Authors:  
Crystal Structures of PF-06438179/GP1111, an Infliximab Biosimilar.,Lerch TF, Sharpe P, Mayclin SJ, Edwards TE, Polleck S, Rouse JC, Zou Q, Conlon HD BioDrugs. 2019 Oct 24. pii: 10.1007/s40259-019-00390-1. doi:, 10.1007/s40259-019-00390-1. PMID:31650490<ref>PMID:31650490</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6ugv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Conlan HD]]
[[Category: Edwards TE]]
[[Category: Lerch TF]]
[[Category: Mayclin SJ]]
[[Category: Polleck S]]
[[Category: Rouse JC]]
[[Category: Sharpe P]]