1l4x
From Proteopedia
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| - | [[Image:1l4x.png|left|200px]] | ||
| - | + | ==octameric de novo designed peptide== | |
| + | <StructureSection load='1l4x' size='340' side='right'caption='[[1l4x]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1l4x]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L4X FirstGlance]. <br> | ||
| + | </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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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=1l4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l4x OCA], [https://pdbe.org/1l4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l4x RCSB], [https://www.ebi.ac.uk/pdbsum/1l4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l4x ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Alpha-helical coiled coils represent a common protein oligomerization motif that are mainly stabilized by hydrophobic interactions occurring along their coiled-coil interface, the so-called hydrophobic seam. We have recently de novo designed and optimized a series of two-heptad repeat long coiled-coil peptides which are further stabilized by a complex network of inter- and intrahelical salt bridges. Here we have extended the de novo design of such two heptad-repeat long peptides by removing the central and most important g-e' Arg to Glu (g-e'RE) ionic interhelical interaction and replacing these residues by alanine residues. The effect of the missing interhelical ionic interaction on coiled-coil formation and stability has been analyzed by CD spectroscopy, analytical ultracentrifugation, and X-ray crystallography. We show that the peptide, while being highly alpha-helical, is no longer able to form a parallel coiled-coil structure but rather assumes an octameric globular helical assembly devoid of any coiled-coil interactions. | ||
| - | + | Removing an interhelical salt bridge abolishes coiled-coil formation in a de novo designed peptide.,Meier M, Lustig A, Aebi U, Burkhard P J Struct Biol. 2002 Jan-Feb;137(1-2):65-72. PMID:12064934<ref>PMID:12064934</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | <div class="pdbe-citations 1l4x" style="background-color:#fffaf0;"></div> |
| - | [[ | + | == References == |
| - | [[Category: Aebi | + | <references/> |
| - | [[Category: Burkhard | + | __TOC__ |
| - | [[Category: Lustig | + | </StructureSection> |
| - | [[Category: Meier | + | [[Category: Large Structures]] |
| - | + | [[Category: Aebi U]] | |
| - | + | [[Category: Burkhard P]] | |
| - | + | [[Category: Lustig A]] | |
| - | + | [[Category: Meier M]] | |
| - | + | ||
Current revision
octameric de novo designed peptide
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