View source for 8v2v


==Solution NMR structure of recifin A [Y6F]==
<StructureSection load='8v2v' size='340' side='right'caption='[[8v2v]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8v2v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Axinella_sp._1_TF-2017 Axinella sp. 1 TF-2017]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8V2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8V2V FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=8v2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8v2v OCA], [https://pdbe.org/8v2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8v2v RCSB], [https://www.ebi.ac.uk/pdbsum/8v2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8v2v ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The peptide recifin A is the inaugural member of the structurally intriguing new fold referred to as a tyrosine-lock. Its central four stranded beta-sheet is stabilized by a unique arrangement in which three disulfide bonds and their interconnecting backbone form a ring that wraps around one of the strands, resulting in a Tyr side chain being buried in the molecular core. Here we aimed to establish a synthetic route to this complex class of natural products. Full length recifin A was successfully generated through native chemical ligation chemistry joining two 21 amino acid residue fragments. Surprisingly, reduced linear recifin A readily adopts the correct, topologically-complex fold via random oxidation of the cysteines, suggesting it is highly energetically favored. Utilizing our synthetic strategy, we generated five recifin A analogues to investigate the structural role of the central Tyr residue and provide the first insights into the structure activity relationship of recifin A towards its cancer target tyrosyl-DNA phosphodiesterase I.

Picking the tyrosine-lock: chemical synthesis of the tyrosyl-DNA phosphodiesterase I inhibitor recifin A and analogues.,Smallwood TB, Krumpe LRH, Payne CD, Klein VG, O'Keefe BR, Clark RJ, Schroeder CI, Rosengren KJ Chem Sci. 2024 Jun 14;15(33):13227-13233. doi: 10.1039/d4sc01976h. eCollection , 2024 Aug 22. PMID:39183914<ref>PMID:39183914</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8v2v" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Axinella sp. 1 TF-2017]]
[[Category: Large Structures]]
[[Category: Payne CD]]
[[Category: Rosengren KJ]]
[[Category: Schroeder CI]]