5hpp: Difference between revisions
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==Crystal structure of a macrocyclic beta-sheet peptide derived from transthyretin (106-121) - (ORN)TIA(MAA)LLS(ORN)S(PHI)STTAV== | |||
<StructureSection load='5hpp' size='340' side='right'caption='[[5hpp]], [[Resolution|resolution]] 2.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hpp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HPP 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]] 2.082Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAA:N-METHYL-L-ALANINE'>MAA</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</scene>, <scene name='pdbligand=PHI:IODO-PHENYLALANINE'>PHI</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=5hpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hpp OCA], [https://pdbe.org/5hpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hpp RCSB], [https://www.ebi.ac.uk/pdbsum/5hpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hpp ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
High-resolution structures of peptide supramolecular assemblies are key to understanding amyloid diseases and designing peptide-based materials. This paper explores the supramolecular assembly of a macrocyclic beta-sheet peptide derived from transthyretin (TTR). The peptide mimics the beta-hairpin formed by the beta-strands G and H of TTR, which form the interface of the TTR tetramer. X-ray crystallography reveals that the peptide does not form a tetramer, but rather assembles to form square channels. The square channels are formed by extended networks of beta-sheets and pack in a "tilted windows" pattern. This unexpected structure represents an emergent property of the peptide and broadens the scope of known supramolecular assemblies of beta-sheets. | |||
Square channels formed by a peptide derived from transthyretin.,Yoo S, Kreutzer AG, Truex NL, Nowick JS Chem Sci. 2016 Dec 1;7(12):6946-6951. doi: 10.1039/c6sc01927g. Epub 2016 Aug 1. PMID:28451128<ref>PMID:28451128</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5hpp" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Yoo | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Kreutzer AG]] | |||
[[Category: Nowick JS]] | |||
[[Category: Yoo S]] | |||
Latest revision as of 10:50, 16 August 2023
Crystal structure of a macrocyclic beta-sheet peptide derived from transthyretin (106-121) - (ORN)TIA(MAA)LLS(ORN)S(PHI)STTAV
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