A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Export

@article{citeulike:2399110, abstract = {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 the tetramer revealed a parallel, four-stranded coiled coil. In the tetramer conformation, the local packing geometry of the two hydrophobic positions in the heptad repeat is reversed relative to that in the dimer. These studies demonstrate that conserved, buried residues in the GCN4 leucine zipper direct dimer formation. In contrast to proposals that the pattern of hydrophobic and polar amino acids in a protein sequence is sufficient to determine three-dimensional structure, the shapes of buried side chains in coiled coils are essential determinants of the global fold.}, address = {Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.}, author = {Harbury, P. B. and Zhang, T. and Kim, P. S. and Alber, T.}, citeulike-article-id = {2399110}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.8248779}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/262/5138/1401}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/8248779}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=8248779}, day = {26}, doi = {10.1126/science.8248779}, issn = {0036-8075}, journal = {Science (New York, N.Y.)}, keywords = {coiled-coil, gcn4, leucine-zipper}, month = {November}, number = {5138}, pages = {1401--1407}, posted-at = {2009-08-28 18:53:01}, priority = {2}, title = {A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants.}, url = {http://dx.doi.org/10.1126/science.8248779}, volume = {262}, year = {1993} }

TY - JOUR ID - citeulike:2399110 L3 - citeulike-article-id:2399110 N2 - 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 the tetramer revealed a parallel, four-stranded coiled coil. In the tetramer conformation, the local packing geometry of the two hydrophobic positions in the heptad repeat is reversed relative to that in the dimer. These studies demonstrate that conserved, buried residues in the GCN4 leucine zipper direct dimer formation. In contrast to proposals that the pattern of hydrophobic and polar amino acids in a protein sequence is sufficient to determine three-dimensional structure, the shapes of buried side chains in coiled coils are essential determinants of the global fold. IS - 5138 JF - Science (New York, N.Y.) SN - 0036-8075 AD - Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115. EP - 1407 TI - A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. VL - 262 SP - 1401 KW - coiled-coil KW - gcn4 KW - leucine-zipper AU - Harbury, PB AU - Zhang, T AU - Kim, PS AU - Alber, T PY - 1993/11/26/ UR - http://dx.doi.org/10.1126/science.8248779 ER -