1coi
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1coi.jpg|left|200px]] | [[Image:1coi.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1coi", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | | | + | {{STRUCTURE_1coi| PDB=1coi | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''DESIGNED TRIMERIC COILED COIL-VALD''' | '''DESIGNED TRIMERIC COILED COIL-VALD''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COI OCA]. | |
==Reference== | ==Reference== | ||
The crystal structure of the designed trimeric coiled coil coil-VaLd: implications for engineering crystals and supramolecular assemblies., Ogihara NL, Weiss MS, Degrado WF, Eisenberg D, Protein Sci. 1997 Jan;6(1):80-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9007979 9007979] | The crystal structure of the designed trimeric coiled coil coil-VaLd: implications for engineering crystals and supramolecular assemblies., Ogihara NL, Weiss MS, Degrado WF, Eisenberg D, Protein Sci. 1997 Jan;6(1):80-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9007979 9007979] | ||
| - | [[Category: Protein complex]] | ||
| - | [[Category: Synthetic construct]] | ||
[[Category: Degrado, W F.]] | [[Category: Degrado, W F.]] | ||
[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
[[Category: Ogihara, N L.]] | [[Category: Ogihara, N L.]] | ||
[[Category: Weiss, M S.]] | [[Category: Weiss, M S.]] | ||
| - | [[Category: | + | [[Category: Alpha-helical bundle]] |
| - | [[Category: | + | [[Category: Coiled coil design]] |
| - | [[Category: | + | [[Category: Protein design]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:56:57 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:56, 2 May 2008
DESIGNED TRIMERIC COILED COIL-VALD
Overview
The three-dimensional structure of the 29-residue designed coiled coil having the amino acid sequence acetyl-E VEALEKK VAALESK VQALEKK VEALEHG-amide has been determined and refined to a crystallographic R-factor of 21.4% for all data from 10-A to 2.1-A resolution. This molecule is called coil-VaLd because it contains valine in the a heptad positions and leucine in the d heptad positions. In the trigonal crystal, three molecules, related by a crystallographic threefold axis, form a parallel three-helix bundle. The bundles are stacked head-to-tail to form a continuous coiled coil along the c-direction of the crystal. The contacts among the three helices within the coiled coil are mainly hydrophobic: four layers of valine residues alternate with four layers of leucine residues to form the core of the bundle. In contrast, mostly hydrophilic contacts mediate the interaction between trimers: here a total of two direct protein--protein hydrogen bonds are found. Based on the structure, we propose a scheme for designing crystals of peptides containing continuous two-, three-, and four-stranded coiled coils.
About this Structure
Full crystallographic information is available from OCA.
Reference
The crystal structure of the designed trimeric coiled coil coil-VaLd: implications for engineering crystals and supramolecular assemblies., Ogihara NL, Weiss MS, Degrado WF, Eisenberg D, Protein Sci. 1997 Jan;6(1):80-8. PMID:9007979 Page seeded by OCA on Fri May 2 12:56:57 2008
