1s9z
From Proteopedia
(Difference between revisions)
| (10 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1s9z.jpg|left|200px]] | ||
| - | + | ==SYNTHETIC 17 AMINO ACID LONG PEPTIDE THAT FORMS A NATIVE-LIKE COILED-COIL AT AMBIENT TEMPERATURE AND AGGREGATES INTO AMYLOID-LIKE FIBRILS AT HIGHER TEMPERATURES.== | |
| - | + | <StructureSection load='1s9z' size='340' side='right'caption='[[1s9z]], [[Resolution|resolution]] 2.01Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[1s9z]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S9Z 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]] 2.01Å</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=NA:SODIUM+ION'>NA</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=1s9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s9z OCA], [https://pdbe.org/1s9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s9z RCSB], [https://www.ebi.ac.uk/pdbsum/1s9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s9z ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | == | + | |
Protein deposition as amyloid fibrils underlies many debilitating human disorders. The complexity and size of disease-related polypeptides, however, often hinders a detailed rational approach to study effects that contribute to the process of amyloid formation. We report here a simplified peptide sequence successfully designed de novo to fold into a coiled-coil conformation under ambient conditions but to transform into amyloid fibrils at elevated temperatures. We have determined the crystal structure of the coiled-coil form and propose a detailed molecular model for the peptide in its fibrillar state. The relative stabilities of the two structural forms and the kinetics of their interconversion were found to be highly sensitive to small sequence changes. The results reveal the importance of specific packing interactions on the kinetics of amyloid formation and show the potential of this exceptionally favorable system for probing details of the molecular origins of amyloid disease. | Protein deposition as amyloid fibrils underlies many debilitating human disorders. The complexity and size of disease-related polypeptides, however, often hinders a detailed rational approach to study effects that contribute to the process of amyloid formation. We report here a simplified peptide sequence successfully designed de novo to fold into a coiled-coil conformation under ambient conditions but to transform into amyloid fibrils at elevated temperatures. We have determined the crystal structure of the coiled-coil form and propose a detailed molecular model for the peptide in its fibrillar state. The relative stabilities of the two structural forms and the kinetics of their interconversion were found to be highly sensitive to small sequence changes. The results reveal the importance of specific packing interactions on the kinetics of amyloid formation and show the potential of this exceptionally favorable system for probing details of the molecular origins of amyloid disease. | ||
| - | + | Exploring amyloid formation by a de novo design.,Kammerer RA, Kostrewa D, Zurdo J, Detken A, Garcia-Echeverria C, Green JD, Muller SA, Meier BH, Winkler FK, Dobson CM, Steinmetz MO Proc Natl Acad Sci U S A. 2004 Mar 30;101(13):4435-40. Epub 2004 Feb 26. PMID:15070736<ref>PMID:15070736</ref> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | Exploring amyloid formation by a de novo design., Kammerer RA, Kostrewa D, Zurdo J, Detken A, Garcia-Echeverria C, Green JD, Muller SA, Meier BH, Winkler FK, Dobson CM, Steinmetz MO | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 1s9z" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Detken A]] | ||
| + | [[Category: Dobson CM]] | ||
| + | [[Category: Garcia-Echeverria C]] | ||
| + | [[Category: Green JD]] | ||
| + | [[Category: Kammerer RA]] | ||
| + | [[Category: Kostrewa D]] | ||
| + | [[Category: Meier BH]] | ||
| + | [[Category: Muller SA]] | ||
| + | [[Category: Steinmetz MO]] | ||
| + | [[Category: Winkler FK]] | ||
| + | [[Category: Zurdo J]] | ||
Current revision
SYNTHETIC 17 AMINO ACID LONG PEPTIDE THAT FORMS A NATIVE-LIKE COILED-COIL AT AMBIENT TEMPERATURE AND AGGREGATES INTO AMYLOID-LIKE FIBRILS AT HIGHER TEMPERATURES.
| |||||||||||
Categories: Large Structures | Detken A | Dobson CM | Garcia-Echeverria C | Green JD | Kammerer RA | Kostrewa D | Meier BH | Muller SA | Steinmetz MO | Winkler FK | Zurdo J
