1kyc
From Proteopedia
(New page: 200px<br /><applet load="1kyc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kyc, resolution 1.45Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1kyc.gif|left|200px]]<br /><applet load="1kyc" size=" | + | [[Image:1kyc.gif|left|200px]]<br /><applet load="1kyc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kyc, resolution 1.45Å" /> | caption="1kyc, resolution 1.45Å" /> | ||
'''CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE STABLIZED BY IONIC INTERACTIONS'''<br /> | '''CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE STABLIZED BY IONIC INTERACTIONS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Alpha-helical coiled coils are a common protein oligomerization motif | + | 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== | ==About this Structure== | ||
| - | 1KYC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with SO4, NH2 and SIN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1KYC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NH2:'>NH2</scene> and <scene name='pdbligand=SIN:'>SIN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KYC OCA]. |
==Reference== | ==Reference== | ||
| Line 23: | Line 23: | ||
[[Category: trimer]] | [[Category: trimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:16 2008'' |
Revision as of 11:39, 21 February 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
1KYC is a Protein complex structure of sequences from [1] with , and as ligands. 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 Thu Feb 21 13:39:16 2008
Categories: Protein complex | Burkhard, P. | Ivaninskii, S. | Lustig, A. | NH2 | SIN | SO4 | Alpha-helix | Coiled coil | De novo design | Trimer
