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3h5f
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3h5f.png|left|200px]] | ||
| - | < | + | ==Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed Peptides.== |
| - | + | <StructureSection load='3h5f' size='340' side='right'caption='[[3h5f]], [[Resolution|resolution]] 1.86Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3h5f]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H5F 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]] 1.86Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LE1:3-SULFANYL-L-VALINE'>LE1</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3h5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h5f OCA], [https://pdbe.org/3h5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h5f RCSB], [https://www.ebi.ac.uk/pdbsum/3h5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h5f ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The effects of switching the chirality of a single layer of amino acids in a three stranded coiled coil has been investigated. X-ray crystallography reveals that this modification is well tolerated and does not alter the designed structure. In contrast, spectroscopic studies of cadmium binding to both the L- and D- enantiomers of the penicillamine, provide evidence that this switch dramatically alters the metal binding capability, the resulting coordination environment and the position of binding. | ||
| - | + | Switching the chirality of the metal environment alters the coordination mode in designed peptides.,Peacock AF, Stuckey JA, Pecoraro VL Angew Chem Int Ed Engl. 2009;48(40):7371-4. doi: 10.1002/anie.200902166. PMID:19579245<ref>PMID:19579245</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3h5f" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | < | + | __TOC__ |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
| - | [[Category: | + | [[Category: Peacock AFA]] |
| - | [[Category: | + | [[Category: Pecoraro VL]] |
| - | [[Category: | + | [[Category: Stuckey JA]] |
| - | [[Category: | + | |
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Current revision
Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed Peptides.
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