The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges Export

@article{citeulike:5624708, abstract = {Background: The parallel two-stranded α-helical coiled coil is the most frequently encountered subunit-oligomerization motif in proteins. The simplicity and regularity of this motif have made it an attractive system to explore some of the fundamental principles of protein folding and stability and to test the principles of de novo design. Results: The X-ray crystal structure of the 18-heptad-repeat α-helical coiled-coil domain of the actin-bundling protein cortexillin I from Dictyostelium discoideum is a tightly packed parallel two-stranded α-helical coiled coil. It harbors a distinct 14-residue sequence motif that is essential for coiled-coil formation, and is a prerequisite for the assembly of cortexillin I. The atomic structure reveals novel types of ionic coiled-coil interactions. In particular, the structure shows that a characteristic interhelical and intrahelical salt-bridge pattern, in combination with the hydrophobic interactions occurring at the dimer interface, is the key structural feature of its coiled-coil trigger site. Conclusions: The knowledge gained from the structure could be used in the de novo design of α-helical coiled coils for applications such as two-stage drug targeting and delivery systems, and in the design of coiled coils as templates for combinatorial helical libraries in drug discovery and as synthetic carrier molecules.}, author = {Burkhard, Peter and Kammerer, Richard A. and Steinmetz, Michel O. and Bourenkov, Gleb P. and Aebi, Ueli}, citeulike-article-id = {5624708}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0969-2126(00)00100-3}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0969212600001003}, doi = {10.1016/S0969-2126(00)00100-3}, issn = {09692126}, journal = {Structure}, keywords = {coiled\_coil}, month = {March}, number = {3}, pages = {223--230}, posted-at = {2009-08-22 13:56:42}, priority = {2}, title = {The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges}, url = {http://dx.doi.org/10.1016/S0969-2126(00)00100-3}, volume = {8}, year = {2000} }

TY - JOUR ID - citeulike:5624708 L3 - citeulike-article-id:5624708 N2 - Background: The parallel two-stranded α-helical coiled coil is the most frequently encountered subunit-oligomerization motif in proteins. The simplicity and regularity of this motif have made it an attractive system to explore some of the fundamental principles of protein folding and stability and to test the principles of de novo design. Results: The X-ray crystal structure of the 18-heptad-repeat α-helical coiled-coil domain of the actin-bundling protein cortexillin I from Dictyostelium discoideum is a tightly packed parallel two-stranded α-helical coiled coil. It harbors a distinct 14-residue sequence motif that is essential for coiled-coil formation, and is a prerequisite for the assembly of cortexillin I. The atomic structure reveals novel types of ionic coiled-coil interactions. In particular, the structure shows that a characteristic interhelical and intrahelical salt-bridge pattern, in combination with the hydrophobic interactions occurring at the dimer interface, is the key structural feature of its coiled-coil trigger site. Conclusions: The knowledge gained from the structure could be used in the de novo design of α-helical coiled coils for applications such as two-stage drug targeting and delivery systems, and in the design of coiled coils as templates for combinatorial helical libraries in drug discovery and as synthetic carrier molecules. IS - 3 JF - Structure SN - 09692126 EP - 230 TI - The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges VL - 8 SP - 223 KW - coiled_coil AU - Burkhard, Peter AU - Kammerer, Richard AU - Steinmetz, Michel AU - Bourenkov, Gleb AU - Aebi, Ueli PY - 2000/03// UR - http://dx.doi.org/10.1016/S0969-2126(00)00100-3 ER -