View source for 7yrw


==Solution structures of a disulfide-directed multicyclic peptide with affinity for HER2==
<StructureSection load='7yrw' size='340' side='right'caption='[[7yrw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yrw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YRW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</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=7yrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yrw OCA], [https://pdbe.org/7yrw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yrw RCSB], [https://www.ebi.ac.uk/pdbsum/7yrw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yrw ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Multicyclic peptides with stable 3D structures are a kind of novel and promising peptide formats for drug design and discovery as they have the potential to combine the best characteristics of small molecules and proteins. However, the development of multicyclic peptides is largely limited to naturally occurring products. It remains a big challenge to develop multicyclic peptides with new structures and functions without recourse to the existing natural scaffolds. Here, we report a general and robust method relying on the utility of new disulfide-directing motifs for designing and discovering diverse multicyclic peptides with potent protein-binding capability. These peptides, referred to as disulfide-directed multicyclic peptides (DDMPs), are tolerant to extensive sequence manipulations and variations of disulfide-pairing frameworks, enabling the development of de novo DDMP libraries useful for ligand and drug discovery. This study opens a new avenue for creating a new generation of multicyclic peptides in sequence and structure space inaccessible by natural scaffolds, thus would greatly benefit the field of peptide drug discovery.

Disulfide-Directed Multicyclic Peptide Libraries for the Discovery of Peptide Ligands and Drugs.,Lu S, Fan S, Xiao S, Li J, Zhang S, Wu Y, Kong C, Zhuang J, Liu H, Zhao Y, Wu C J Am Chem Soc. 2023 Jan 25;145(3):1964-1972. doi: 10.1021/jacs.2c12462. Epub 2023 , Jan 12. PMID:36633218<ref>PMID:36633218</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7yrw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Fan SH]]
[[Category: Wu CL]]