3u6r: Difference between revisions

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<StructureSection load='3u6r' size='340' side='right'caption='[[3u6r]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
<StructureSection load='3u6r' size='340' side='right'caption='[[3u6r]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3u6r]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U6R FirstGlance]. <br>
<table><tr><td colspan='2'>[[3u6r]] 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=3U6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U6R FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.67&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3u6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u6r OCA], [https://pdbe.org/3u6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u6r RCSB], [https://www.ebi.ac.uk/pdbsum/3u6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u6r 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=3u6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u6r OCA], [https://pdbe.org/3u6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u6r RCSB], [https://www.ebi.ac.uk/pdbsum/3u6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u6r ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Single-chain variable fragment (scFvs) antibodies are small polypeptides ( approximately 26 kD) containing the heavy (V(H)) and light (V(L)) immunoglobulin domains of a parent antibody connected by a flexible linker. In addition to being frequently used in diagnostics and therapy for an increasing number of human diseases, scFvs are important tools for structural biology as crystallization chaperones. Although scFvs can be expressed in many different organisms, the expression level of an scFv strongly depends on its particular amino acid sequence. We report here a system allowing for easy and efficient cloning of (i) scFvs selected by phage display and (ii) individual heavy and light chain sequences from hybridoma cDNA into expression plasmids engineered for secretion of the recombinant fragment produced in Drosophila S2 cells. We validated the method by producing five scFvs derived from human and murine parent antibodies directed against various antigens. The production yields varied between 5 and 12 mg monomeric scFv per liter of supernatant, indicating a relative independence on the individual sequences. The recombinant scFvs bound their cognate antigen with high affinity, comparable with the parent antibodies. The suitability of the produced recombinant fragments for structural studies was demonstrated by crystallization and structure determination of one of the produced scFvs, derived from a broadly neutralizing antibody against the major glycoprotein E2 of the hepatitis C virus. Structural comparison with the Protein Data Bank revealed the typical spatial organization of V(H) and V(L) domains, further validating the here-reported expression system.
High-level secretion of recombinant monomeric murine and human single-chain Fv antibodies from Drosophila S2 cells.,Gilmartin AA, Lamp B, Rumenapf T, Persson MA, Rey FA, Krey T Protein Eng Des Sel. 2011 Dec 17. PMID:22160929<ref>PMID:22160929</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3u6r" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
*[[3D structures of human antibody|3D structures of human antibody]]
*[[3D structures of human antibody|3D structures of human antibody]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gilmartin, A A]]
[[Category: Gilmartin AA]]
[[Category: Krey, T]]
[[Category: Krey T]]
[[Category: Lamp, B]]
[[Category: Lamp B]]
[[Category: Persson, A A]]
[[Category: Persson AA]]
[[Category: Rey, F A]]
[[Category: Rey FA]]
[[Category: Ruemenapf, T]]
[[Category: Ruemenapf T]]
[[Category: Ig-like domain]]
[[Category: Immune system]]
[[Category: Neutralizing single chain fv]]
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