5dtf: Difference between revisions
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<StructureSection load='5dtf' size='340' side='right'caption='[[5dtf]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5dtf' size='340' side='right'caption='[[5dtf]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5dtf]] is a 5 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5dtf]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DTF FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CT:HYPUSINE'>5CT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dtf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dtf OCA], [https://pdbe.org/5dtf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dtf RCSB], [https://www.ebi.ac.uk/pdbsum/5dtf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dtf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/IGHG_RABIT IGHG_RABIT] | |||
<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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Oryctolagus cuniculus]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Carter PJ]] | ||
[[Category: | [[Category: Zhai Q]] | ||
Latest revision as of 00:58, 29 June 2023
context-independent anti-hypusine antibody FabHpu98.61 in complex with hypusinecontext-independent anti-hypusine antibody FabHpu98.61 in complex with hypusine
Structural highlights
FunctionPublication Abstract from PubMedContext-independent anti-hypusine antibodies that bind to the post-translational modification (PTM), hypusine, with minimal dependence on flanking amino acid sequences, were identified. The antibodies bind to both hypusine and deoxyhypusine or selectively to hypusine but not to deoxyhypusine. Phage display was used to further enhance the affinity of the antibodies. Affinity maturation of these anti-hypusine antibodies improved their performance in affinity capture of the only currently known hypusinated protein, eukaryotic translation initiation factor 5A. These anti-hypusine antibodies may have utility in the identification of novel hypusinated proteins. Crystal structures of the corresponding Fab fragments were determined in complex with hypusine- or deoxyhypusine-containing peptides. The hypusine or deoxyhypusine moiety was found to reside in a deep pocket formed between VH and VL domains of the Fab fragments. Interaction between the antibodies and hypusine includes an extensive hydrogen bond network. These are, to our knowledge, the first reported structures of context-independent anti-PTM antibodies in complex with the corresponding PTM. Structural Analysis and Optimization of Context-Independent Anti-Hypusine Antibodies.,Zhai Q, He M, Song A, Deshayes K, Dixit VM, Carter PJ J Mol Biol. 2016 Jan 14. pii: S0022-2836(16)00025-5. doi:, 10.1016/j.jmb.2016.01.006. PMID:26778617[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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