1l4x: Difference between revisions
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[[Image:1l4x.gif|left|200px]] | [[Image:1l4x.gif|left|200px]] | ||
'''octameric de novo designed peptide''' | {{Structure | ||
|PDB= 1l4x |SIZE=350|CAPTION= <scene name='initialview01'>1l4x</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> and <scene name='pdbligand=SIN:SUCCINIC ACID'>SIN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''octameric de novo designed peptide''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1L4X is a [ | 1L4X is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4X OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12064934 12064934] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Aebi, U.]] | [[Category: Aebi, U.]] | ||
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[[Category: SIN]] | [[Category: SIN]] | ||
[[Category: coiled coil]] | [[Category: coiled coil]] | ||
[[Category: ionic | [[Category: ionic interaction]] | ||
[[Category: protein de novo design]] | [[Category: protein de novo design]] | ||
[[Category: protein folding]] | [[Category: protein folding]] | ||
[[Category: protein oligomerization]] | [[Category: protein oligomerization]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:26:24 2008'' | ||
Revision as of 10:26, 20 March 2008
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| 1l4x, resolution 2.00Å | |||||||||||||
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| Ligands: | MG, CL, NH2 and SIN | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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]. 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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