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1l4x
From Proteopedia
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|PDB= 1l4x |SIZE=350|CAPTION= <scene name='initialview01'>1l4x</scene>, resolution 2.00Å | |PDB= 1l4x |SIZE=350|CAPTION= <scene name='initialview01'>1l4x</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1d7m|1D7M]], [[1hqj|1HQJ]], [[1kyc|1KYC]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l4x OCA], [http://www.ebi.ac.uk/pdbsum/1l4x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l4x RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Lustig, A.]] | [[Category: Lustig, A.]] | ||
[[Category: Meier, M.]] | [[Category: Meier, M.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NH2]] | ||
| - | [[Category: SIN]] | ||
[[Category: coiled coil]] | [[Category: coiled coil]] | ||
[[Category: ionic interaction]] | [[Category: ionic interaction]] | ||
| Line 35: | Line 34: | ||
[[Category: protein oligomerization]] | [[Category: protein oligomerization]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:58:03 2008'' |
Revision as of 18:58, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1D7M, 1HQJ, 1KYC
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 21:58:03 2008
