1s9z

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.

spinqualitylabelsall models 1s9z, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1s9z is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.01Å Ligands: ACE, NA, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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