1kyc
From Proteopedia
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[[Image:1kyc.gif|left|200px]] | [[Image:1kyc.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE STABLIZED BY IONIC INTERACTIONS''' | '''CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE STABLIZED BY IONIC INTERACTIONS''' | ||
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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=1KYC OCA]. | |
==Reference== | ==Reference== | ||
Improving coiled-coil stability by optimizing ionic interactions., Burkhard P, Ivaninskii S, Lustig A, J Mol Biol. 2002 May 3;318(3):901-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12054832 12054832] | Improving coiled-coil stability by optimizing ionic interactions., Burkhard P, Ivaninskii S, Lustig A, J Mol Biol. 2002 May 3;318(3):901-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12054832 12054832] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Burkhard, P.]] | [[Category: Burkhard, P.]] | ||
[[Category: Ivaninskii, S.]] | [[Category: Ivaninskii, S.]] | ||
[[Category: Lustig, A.]] | [[Category: Lustig, A.]] | ||
| - | [[Category: | + | [[Category: Alpha-helix]] |
| - | [[Category: | + | [[Category: Coiled coil]] |
| - | [[Category: | + | [[Category: De novo design]] |
| - | [[Category: | + | [[Category: Trimer]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:19:20 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:19, 2 May 2008
CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE STABLIZED BY IONIC INTERACTIONS
Overview
Alpha-helical coiled coils are a common protein oligomerization motif stabilized mainly by hydrophobic interactions occurring along the coiled-coil interface. We have recently designed and solved the structure of a two-heptad repeat coiled-coil peptide that is stabilized further by a complex network of inter- and intrahelical salt-bridges in addition to the hydrophobic interactions. Here, we extend and improve the de novo design of this two heptad-repeat peptide by four newly designed peptides characterized by different types of ionic interactions. The contribution of these different types of ionic interactions to coiled-coil stability are analyzed by CD spectroscopy and analytical ultracentrifugation. We show that all peptides are highly alpha-helical and two of them are 100% dimeric under physiological conditions. Furthermore, we have solved the X-ray structure of the most stable of these peptides and the rational design principles are verified by comparing this structure to the structure of the parent peptide. We show that by combining the most favorable inter- and intrahelical salt-bridge arrangements it is possible to design coiled-coil oligomerization domains with improved stability properties.
About this Structure
Full crystallographic information is available from OCA.
Reference
Improving coiled-coil stability by optimizing ionic interactions., Burkhard P, Ivaninskii S, Lustig A, J Mol Biol. 2002 May 3;318(3):901-10. PMID:12054832 Page seeded by OCA on Fri May 2 23:19:20 2008
