1l4x: Difference between revisions
New page: left|200px<br /><applet load="1l4x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l4x, resolution 2.00Å" /> '''octameric de novo de... |
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[[Image:1l4x.gif|left|200px]]<br /><applet load="1l4x" size=" | [[Image:1l4x.gif|left|200px]]<br /><applet load="1l4x" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1l4x, resolution 2.00Å" /> | caption="1l4x, resolution 2.00Å" /> | ||
'''octameric de novo designed peptide'''<br /> | '''octameric de novo designed peptide'''<br /> | ||
==Overview== | ==Overview== | ||
Alpha-helical coiled coils represent a common protein oligomerization | Alpha-helical coiled coils represent a common protein oligomerization motif that are mainly stabilized by hydrophobic interactions occurring along their coiled-coil interface, the so-called hydrophobic seam. We have recently de novo designed and optimized a series of two-heptad repeat long coiled-coil peptides which are further stabilized by a complex network of inter- and intrahelical salt bridges. Here we have extended the de novo design of such two heptad-repeat long peptides by removing the central and most important g-e' Arg to Glu (g-e'RE) ionic interhelical interaction and replacing these residues by alanine residues. The effect of the missing interhelical ionic interaction on coiled-coil formation and stability has been analyzed by CD spectroscopy, analytical ultracentrifugation, and X-ray crystallography. We show that the peptide, while being highly alpha-helical, is no longer able to form a parallel coiled-coil structure but rather assumes an octameric globular helical assembly devoid of any coiled-coil interactions. | ||
==About this Structure== | ==About this Structure== | ||
1L4X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with MG, CL, NH2 and SIN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1L4X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</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=1L4X OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: protein oligomerization]] | [[Category: protein oligomerization]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:19 2008'' | ||
Revision as of 11:41, 21 February 2008
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octameric de novo designed peptide
Overview
Alpha-helical coiled coils represent a common protein oligomerization motif that are mainly stabilized by hydrophobic interactions occurring along their coiled-coil interface, the so-called hydrophobic seam. We have recently de novo designed and optimized a series of two-heptad repeat long coiled-coil peptides which are further stabilized by a complex network of inter- and intrahelical salt bridges. Here we have extended the de novo design of such two heptad-repeat long peptides by removing the central and most important g-e' Arg to Glu (g-e'RE) ionic interhelical interaction and replacing these residues by alanine residues. The effect of the missing interhelical ionic interaction on coiled-coil formation and stability has been analyzed by CD spectroscopy, analytical ultracentrifugation, and X-ray crystallography. We show that the peptide, while being highly alpha-helical, is no longer able to form a parallel coiled-coil structure but rather assumes an octameric globular helical assembly devoid of any coiled-coil interactions.
About this Structure
1L4X is a Protein complex structure of sequences from [1] with MG, CL, NH2 and SIN as ligands. Full crystallographic information is available from OCA.
Reference
Removing an interhelical salt bridge abolishes coiled-coil formation in a de novo designed peptide., Meier M, Lustig A, Aebi U, Burkhard P, J Struct Biol. 2002 Jan-Feb;137(1-2):65-72. PMID:12064934
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