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'''DESIGNED TRIMERIC COILED COIL-VALD''' | '''DESIGNED TRIMERIC COILED COIL-VALD''' | ||
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==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: 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
