Rational Analysis of Coiled-Coil Packing Specificity Using the Knob-Socket Model
Poster Number
03B
Format
Poster Presentation
Faculty Mentor Name
Jerry Tsai
Faculty Mentor Department
Chemistry
Additional Faculty Mentor Name
Hyun Joo
Additional Faculty Mentor Department
Chemistry
Abstract/Artist Statement
Identifying the interactions that exist in the leucine zipper DNA binding proteins are crucial for the understanding of disease formation, proliferation, and the development of combative measures against these diseases. Use of the Knob-Socket model for determination of packing structure provides a novel approach to analyze protein-protein as well as protein-nucleic acid interactions. A Knob-Socket analysis of the protein-protein interface provides unique insight into the classical leucine zipper pseudo-7mer repeat. A deeper analysis of longer leucine zippers shows unique packing patterns not indicated by classical representations like the helical wheel. From analysis of the Knob-Socket packing maps, this research provides evidence of a general framework for defining the specificity between coiled coils. Generally, the patterns follow classic Crick knob-into-holes packing. However, the Knob-Socket maps show how hydrophobic specificity is defined in the coiled coil interface, where knobs are centralized in the middle of the socket packing, while the peripheral socket residues are hydrophilic. Furthermore, the bias of the filled over free propensities shows a clear pattern that explains the specificity of a set of hydrophobic interactions. This research presents a clear model for the coiled-coil interaction and provides the basis for further exploration into these interactions to improve our understanding of disease formation and eventually develop techniques against these diseases.
Location
DeRosa University Center, Ballroom
Start Date
28-4-2018 1:00 PM
End Date
28-4-2018 3:00 PM
Rational Analysis of Coiled-Coil Packing Specificity Using the Knob-Socket Model
DeRosa University Center, Ballroom
Identifying the interactions that exist in the leucine zipper DNA binding proteins are crucial for the understanding of disease formation, proliferation, and the development of combative measures against these diseases. Use of the Knob-Socket model for determination of packing structure provides a novel approach to analyze protein-protein as well as protein-nucleic acid interactions. A Knob-Socket analysis of the protein-protein interface provides unique insight into the classical leucine zipper pseudo-7mer repeat. A deeper analysis of longer leucine zippers shows unique packing patterns not indicated by classical representations like the helical wheel. From analysis of the Knob-Socket packing maps, this research provides evidence of a general framework for defining the specificity between coiled coils. Generally, the patterns follow classic Crick knob-into-holes packing. However, the Knob-Socket maps show how hydrophobic specificity is defined in the coiled coil interface, where knobs are centralized in the middle of the socket packing, while the peripheral socket residues are hydrophilic. Furthermore, the bias of the filled over free propensities shows a clear pattern that explains the specificity of a set of hydrophobic interactions. This research presents a clear model for the coiled-coil interaction and provides the basis for further exploration into these interactions to improve our understanding of disease formation and eventually develop techniques against these diseases.