7l98
From Proteopedia
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<StructureSection load='7l98' size='340' side='right'caption='[[7l98]]' scene=''> | <StructureSection load='7l98' size='340' side='right'caption='[[7l98]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[7l98]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7L98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L98 FirstGlance]. <br> |
| - | </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=7l98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l98 OCA], [https://pdbe.org/7l98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l98 RCSB], [https://www.ebi.ac.uk/pdbsum/7l98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l98 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ITZ:2-[(1S,2S)-1-amino-2-methylbutyl]-1,3-thiazole-4-carboxylic+acid'>ITZ</scene>, <scene name='pdbligand=MEA:N-METHYLPHENYLALANINE'>MEA</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=7l98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l98 OCA], [https://pdbe.org/7l98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l98 RCSB], [https://www.ebi.ac.uk/pdbsum/7l98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l98 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | N- or C-methylation in natural and synthetic cyclic peptides can increase membrane permeability, but it remains unclear why this happens in some cases but not others. Here we compare three-dimensional structures for cyclic peptides from six families, including isomers differing only in the location of an N- or Calpha-methyl substituent. We show that a single methyl group only increases membrane permeability when it connects or expands hydrophobic surface patches. Positional isomers, with the same molecular weight, hydrogen bond donors/acceptors, rotatable bonds, calculated LogP, topological polar surface area, and total hydrophobic surface area, can have different membrane permeabilities that correlate with the size of the largest continuous hydrophobic surface patch. These results illuminate a key local molecular determinant of membrane permeability. | ||
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| + | Connecting Hydrophobic Surfaces in Cyclic Peptides Increases Membrane Permeability.,Hoang HN, Hill TA, Fairlie DP Angew Chem Int Ed Engl. 2021 Apr 6;60(15):8385-8390. doi: 10.1002/anie.202012643., Epub 2021 Mar 4. PMID:33185961<ref>PMID:33185961</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7l98" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hoang HN]] | [[Category: Hoang HN]] | ||
Current revision
Connecting hydrophobic surfaces in cyclic peptides increases membrane permeability
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