1s9z
From Proteopedia
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'''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.''' | '''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.''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S9Z OCA]. | |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/15070736 15070736] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15070736 15070736] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Detken, A.]] | [[Category: Detken, A.]] | ||
[[Category: Dobson, C M.]] | [[Category: Dobson, C M.]] | ||
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[[Category: Winkler, F K.]] | [[Category: Winkler, F K.]] | ||
[[Category: Zurdo, J.]] | [[Category: Zurdo, J.]] | ||
| - | [[Category: | + | [[Category: Coiled coil]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:28:10 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:28, 3 May 2008
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
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 Sat May 3 08:28:10 2008
