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| {{STRUCTURE_1coi| PDB=1coi | SCENE= }} | | {{STRUCTURE_1coi| PDB=1coi | SCENE= }} |
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| '''DESIGNED TRIMERIC COILED COIL-VALD'''
| | ===DESIGNED TRIMERIC COILED COIL-VALD=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_9007979}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9007979 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9007979}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Coiled coil design]] | | [[Category: Coiled coil design]] |
| [[Category: Protein design]] | | [[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 Mon Jun 30 21:01:27 2008'' |
