Publication Date:
1993-02-26
Description:
The x-ray crystal structure of a peptide designed to form a double-stranded parallel coiled coil shows that it is actually a triple-stranded coiled coil formed by three alpha-helices. Unlike the designed parallel coiled coil, the helices run up-up-down. The structure is stabilized by a distinctive hydrophobic interface consisting of eight layers. As in the design, each alpha-helix in the coiled coil contributes one leucine side chain to each layer. The structure suggests that hydrophobic interactions are a dominant factor in the stabilization of coiled coils. The stoichiometry and geometry of coiled coils are primarily determined by side chain packing in the solvent-inaccessible interior, but electrostatic interactions also contribute.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lovejoy, B -- Choe, S -- Cascio, D -- McRorie, D K -- DeGrado, W F -- Eisenberg, D -- 31299/PHS HHS/ -- New York, N.Y. -- Science. 1993 Feb 26;259(5099):1288-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, University of California, Los Angeles 90024-1570.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8446897" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Crystallography
;
*DNA-Binding Proteins
;
Fungal Proteins/chemistry/ultrastructure
;
Hydrogen Bonding
;
Leucine/chemistry
;
Models, Molecular
;
Molecular Sequence Data
;
Peptides/chemistry
;
Protein Kinases/chemistry/ultrastructure
;
*Protein Structure, Secondary
;
*Saccharomyces cerevisiae Proteins
;
Tropomyosin/chemistry/ultrastructure
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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