STRUCTURAL STUDIES OF NATIVE AND DESIGNED ALPHA HELICAL COILED COILS

Cornell University, Ithaca NY

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Abstract

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Research in the Keating lab aims to understand determinants of structural specificity and interaction specificity in alpha-helical coiled coils, a common interaction motif in the proteome. We apply an integrated program of experimental measurement, computational analysis, and structure determinantion. Targets of particular interest include bZIP transcription factors and coiled coils of the yeast spindle pole body. For the bZIPs, combinatorial interactions that regulate transcription are made via coiled-coil dimers. We are studying both native and synthetic coiled-coil peptides that interact with human bZIPs by forming coiled-coil dimers. Proteins of the spindle pole body are highly enriched in predicted coiled-coil domains, and we are characterizing these as part of an effort to build models of the overall structure of the very large spindle pole body assembly.