9bnh: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: '''Unreleased structure''' The entry 9bnh is ON HOLD Authors: Description: Category: Unreleased Structures |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==X-ray Crystal Structure of Cu-TZ4H tryptophan Zipper Metallo-Peptide== | |||
<StructureSection load='9bnh' size='340' side='right'caption='[[9bnh]], [[Resolution|resolution]] 1.12Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9bnh]] is a 2 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=9BNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BNH 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]] 1.12Å</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=9bnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bnh OCA], [https://pdbe.org/9bnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bnh RCSB], [https://www.ebi.ac.uk/pdbsum/9bnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bnh ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Metal binding to beta-sheets occurs in many metalloproteins and is also implicated in the pathology of Alzheimer's disease. De novo designed metallo-beta-sheets have been pursued as models and mimics of these proteins. However, no crystal structures of canonical beta-sheet metallopeptides have yet been obtained, in stark contrast to many examples for a-helical metallopeptides, leading to a poor understanding for their chemistry. To address this, we have engineered tryptophan zippers, stable 12-residue beta-sheet peptides, to bind Cu(II) ions and obtained crystal structures through single crystal X-ray diffraction (SC-XRD). We find that metal binding triggers several unexpected supramolecular assemblies that demonstrate the range of higher-order structures available to metallo-beta-sheets. Overall, these findings underscore the importance of crystallography in elucidating the rich structural landscape of metallo-beta-sheet peptides. | |||
Crystallography reveals metal-triggered restructuring of beta-hairpins.,Dang VT, Engineer A, McElheny D, Drena A, Telser J, Tomczak K, Nguyen AI Chemistry. 2024 Aug 16:e202402101. doi: 10.1002/chem.202402101. PMID:39152095<ref>PMID:39152095</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9bnh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Dang VT]] | |||
[[Category: Nguyen A]] | |||
Latest revision as of 05:44, 4 September 2024
X-ray Crystal Structure of Cu-TZ4H tryptophan Zipper Metallo-Peptide
| ||||||||||||
