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1l4x

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(New page: 200px<br /><applet load="1l4x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l4x, resolution 2.00&Aring;" /> '''octameric de novo de...)
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[[Image:1l4x.gif|left|200px]]<br /><applet load="1l4x" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l4x.gif|left|200px]]<br /><applet load="1l4x" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1l4x, resolution 2.00&Aring;" />
caption="1l4x, resolution 2.00&Aring;" />
'''octameric de novo designed peptide'''<br />
'''octameric de novo designed peptide'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L4X OCA].
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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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:30:11 2007''
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''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

Image:1l4x.gif

1l4x, resolution 2.00Å

Drag the structure with the mouse to rotate

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 , , and 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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