1s9z
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1s9z |SIZE=350|CAPTION= <scene name='initialview01'>1s9z</scene>, resolution 2.01Å | |PDB= 1s9z |SIZE=350|CAPTION= <scene name='initialview01'>1s9z</scene>, resolution 2.01Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s9z OCA], [http://www.ebi.ac.uk/pdbsum/1s9z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s9z RCSB]</span> | ||
}} | }} | ||
| Line 32: | Line 35: | ||
[[Category: Winkler, F K.]] | [[Category: Winkler, F K.]] | ||
[[Category: Zurdo, J.]] | [[Category: Zurdo, J.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: ZN]] | ||
[[Category: coiled coil]] | [[Category: coiled coil]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:39:20 2008'' |
Revision as of 20:39, 30 March 2008
| |||||||
| , resolution 2.01Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
Overview
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.
About this Structure
1S9Z is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 23:39:20 2008
