View source for 7lib


==X-ray crystal structure of a cyclic peptide containing beta-2-microglobulin (63-69) and a gamma-methylornithine turn unit==
<StructureSection load='7lib' size='340' side='right'caption='[[7lib]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7lib]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LIB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</scene>, <scene name='pdbligand=PHI:IODO-PHENYLALANINE'>PHI</scene>, <scene name='pdbligand=Y1V:(4R)-5-amino-L-leucine'>Y1V</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=7lib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lib OCA], [https://pdbe.org/7lib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lib RCSB], [https://www.ebi.ac.uk/pdbsum/7lib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lib ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Although beta-hairpins are widespread in proteins, there is still no universal tool to coax any small peptide to adopt a beta-hairpin conformation, regardless of sequence. Here, we report that delta-linked gamma( R )-methyl-ornithine ( delta MeOrn) provides an improved beta-turn template for inducing a beta-hairpin conformation in peptides. We have developed a synthesis of protected delta MeOrn as a building block suitable for use in Fmoc-based solid-phase peptide synthesis. The synthesis begins with l -leucine and affords gram quantities of the N alpha -Boc- N delta -Fmoc-gamma( R )-methyl-ornithine building block. X-ray crystallography confirms that the delta MeOrn turn unit adopts a folded structure in a macrocyclic beta-hairpin peptide. CD and NMR spectroscopic experiments allow comparison of the delta MeOrn turn template to the delta-linked ornithine ( delta Orn) turn template that our laboratory has previously introduced and also to the popular d -Pro-Gly turn template. Collectively, these studies demonstrate that the folding of the delta MeOrn turn template is substantially better than that of delta Orn and is comparable to d -Pro-Gly.

An Improved Turn Structure for Inducing beta-Hairpin Formation in Peptides.,Nowick JS, Li X, Sabol AL, Wierzbicki M, Salveson PJ Angew Chem Int Ed Engl. 2021 Jul 13. doi: 10.1002/anie.202105559. PMID:34258835<ref>PMID:34258835</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7lib" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Li X]]
[[Category: Nowick JS]]
[[Category: Wierzbicki M]]