Buried polar residues in coiled-coil interfaces. Export

@article{citeulike:4156121, abstract = {Coiled coils, estimated to constitute 3-5\% of the encoded residues in most genomes, are characterized by a heptad repeat, (abcdefg)(n), where the buried a and d positions form the interface between multiple alpha-helices. Although generally hydrophobic, a substantial fraction ( approximately 20\%) of these a- and d-position residues are polar or charged. We constructed variants of the well-characterized coiled coil GCN4-p1 with a single polar residue (Asn, Gln, Ser, or Thr) at either an a or a d position. The stability and oligomeric specificity of each variant were measured, and crystal structures of coiled-coil trimers with threonine or serine at either an a or a d position were determined. The structures show how single polar residues in the interface affect not only local packing, but also overall coiled-coil geometry as seen by changes in the Crick supercoil parameters and core cavity volumes.}, author = {Akey, D. L. and Malashkevich, V. N. and Kim, P. S.}, citeulike-article-id = {4156121}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/11371197}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=11371197}, day = {29}, issn = {0006-2960}, journal = {Biochemistry}, keywords = {coiled-coil, gcn4, leucine-zipper}, month = {May}, number = {21}, pages = {6352--6360}, posted-at = {2009-08-28 18:29:38}, priority = {2}, title = {Buried polar residues in coiled-coil interfaces.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/11371197}, volume = {40}, year = {2001} }

TY - JOUR ID - citeulike:4156121 L3 - citeulike-article-id:4156121 N2 - Coiled coils, estimated to constitute 3-5% of the encoded residues in most genomes, are characterized by a heptad repeat, (abcdefg)(n), where the buried a and d positions form the interface between multiple alpha-helices. Although generally hydrophobic, a substantial fraction ( approximately 20%) of these a- and d-position residues are polar or charged. We constructed variants of the well-characterized coiled coil GCN4-p1 with a single polar residue (Asn, Gln, Ser, or Thr) at either an a or a d position. The stability and oligomeric specificity of each variant were measured, and crystal structures of coiled-coil trimers with threonine or serine at either an a or a d position were determined. The structures show how single polar residues in the interface affect not only local packing, but also overall coiled-coil geometry as seen by changes in the Crick supercoil parameters and core cavity volumes. IS - 21 JF - Biochemistry SN - 0006-2960 EP - 6360 TI - Buried polar residues in coiled-coil interfaces. VL - 40 SP - 6352 KW - coiled-coil KW - gcn4 KW - leucine-zipper AU - Akey, DL AU - Malashkevich, VN AU - Kim, PS PY - 2001/05/29/ UR - http://view.ncbi.nlm.nih.gov/pubmed/11371197 ER -