Antiparallel Four-Stranded Coiled Coil Specified by a 3-3-1 Hydrophobic Heptad Repeat
نویسندگان
چکیده
منابع مشابه
X-ray crystal structure of a TRPM assembly domain reveals an antiparallel four-stranded coiled-coil.
Transient receptor potential (TRP) channels comprise a large family of tetrameric cation-selective ion channels that respond to diverse forms of sensory input. Earlier studies showed that members of the TRPM subclass possess a self-assembling tetrameric C-terminal cytoplasmic coiled-coil domain that underlies channel assembly and trafficking. Here, we present the high-resolution crystal structu...
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The study and successful design of coiled-coil protein structural motifs have provided much insight into the rules governing protein folding and stability. In this work we use a thermodynamic approach to quantitate the rules that govern the specific oligomerization of coiled coils. We have designed a highly stable trimeric coiled coil by placing valine residues at each a position and leucine re...
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Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of ...
متن کاملLeucine Zipper Mutants
Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of ...
متن کاملElectrostatic determinants of stability in parallel 3-stranded coiled coils.
The optimal positioning of salt-bridging interactions in a parallel alpha-helical homotrimeric coiled coil has been explored in a metal ion-assembled polypeptide trimer of 60 residues; arginine-glutamate pairs are more stabilizing than the corresponding lysine-glutamate pairs, and optimal stabilization is obtained with positively charged arginine residues at the c positions of the alpha-helical...
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ژورنال
عنوان ژورنال: Structure
سال: 2006
ISSN: 0969-2126
DOI: 10.1016/j.str.2005.10.010