4x0s: Difference between revisions
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==Hexamer formed by a macrocycle containing a sequence from beta-2-microglobulin (63-69).== | ==Hexamer formed by a macrocycle containing a sequence from beta-2-microglobulin (63-69).== | ||
<StructureSection load='4x0s' size='340' side='right' caption='[[4x0s]], [[Resolution|resolution]] 2.03Å' scene=''> | <StructureSection load='4x0s' size='340' side='right' caption='[[4x0s]], [[Resolution|resolution]] 2.03Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x0s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x0s RCSB], [http://www.ebi.ac.uk/pdbsum/4x0s PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x0s OCA], [http://pdbe.org/4x0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x0s RCSB], [http://www.ebi.ac.uk/pdbsum/4x0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x0s ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4x0s" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 04:49, 10 March 2017
Hexamer formed by a macrocycle containing a sequence from beta-2-microglobulin (63-69).Hexamer formed by a macrocycle containing a sequence from beta-2-microglobulin (63-69).
Structural highlights
Publication Abstract from PubMedAmyloid diseases such as Alzheimer's disease, Parkinson's disease, and type II diabetes share common features of toxic soluble protein oligomers. There are no structures at atomic resolution of oligomers formed by full-length amyloidogenic peptides and proteins, and only a few structures of oligomers formed by peptide fragments. The paucity of structural information provides a fundamental roadblock to understanding the pathology of amyloid diseases and developing preventions or therapies. Here, we present the X-ray crystallographic structures of three families of oligomers formed by macrocyclic peptides containing a heptapeptide sequence derived from the amyloidogenic E chain of beta2-microglobulin (beta2m). Each macrocyclic peptide contains the heptapeptide sequence beta2m63-69 and a second heptapeptide sequence containing an N-methyl amino acid. These peptides form beta-sheets that further associate into hexamers, octamers, and dodecamers: the hexamers are trimers of dimers; the octamers are tetramers of dimers; and the dodecamers contain two trimer subunits surrounded by three pairs of beta-sheets. These structures illustrate a common theme in which dimer and trimer subunits further associate to form a hydrophobic core. The seven X-ray crystallographic structures not only illustrate a range of oligomers that a single amyloidogenic peptide sequence can form, but also how mutation can alter the size and topology of the oligomers. A cocrystallization experiment in which a dodecamer-forming peptide recruits a hexamer-forming peptide to form mixed dodecamers demonstrates that one species can dictate the oligomerization of another. These findings should also be relevant to the formation of oligomers of full-length peptides and proteins in amyloid diseases. X-ray Crystallographic Structures of Oligomers of Peptides Derived from beta-Microglobulin.,Spencer RK, Kreutzer AG, Salveson PJ, Li H, Nowick JS J Am Chem Soc. 2015 May 12. PMID:25915729[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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