8uo7

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Current revision (14:57, 6 November 2024) (edit) (undo)
 
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
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== Publication Abstract from PubMed ==
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Engineering biosynthetic pathways to ribosomally synthesized and post-translationally modified peptides (RiPPs) offers several advantages for both in vivo and in vitro applications. Here we probe the ability of peptide cyclases to generate trimacrocycle microviridin analogs with non-native cross-links. The results demonstrate that diverse chemistries are tolerated by macrocyclases in the ATP-grasp family and allow for the construction of unique cyclic peptide architectures that retain protease inhibition activity. In addition, cocomplex structures of analogs bound to a model protease were determined, illustrating how changes in functional groups maintain peptide conformation and target binding.
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Alternative Linkage Chemistries in the Chemoenzymatic Synthesis of Microviridin-Based Cyclic Peptides.,Patel KP, Chen WT, Delbecq L, Bruner SD Org Lett. 2024 Feb 16;26(6):1138-1142. doi: 10.1021/acs.orglett.3c04045. Epub , 2024 Feb 2. PMID:38306609<ref>PMID:38306609</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8uo7" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Bovine trypsin in complex with deacetylated wild type microviridin J

PDB ID 8uo7

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