Title

Rational Analysis of Coiled-Coil Packing Specificity Using the Knob-Socket Model

Poster Number

03B

Lead Author Major

Biochemistry

Lead Author Status

Junior

Second Author Major

Biochemistry

Second Author Status

Junior

Third Author Major

Biochemistry

Third Author Status

Junior

Fourth Author Major

Chemistry

Fourth Author Status

Junior

Format

Poster Presentation

Faculty Mentor Name

Jerry Tsai

Faculty Mentor Email

jtsai@pacific.edu

Faculty Mentor Department

Chemistry

Additional Faculty Mentor Name

Hyun Joo

Additional Faculty Mentor Email

hjoo@pacific.edu

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

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Apr 28th, 1:00 PM Apr 28th, 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.