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Analyzing the Three Dimensional Structure of Cortactin Protein
Author(s) -
Gurumani Margaret,
Kruchten Anne
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.792.24
Subject(s) - cortactin , calpain , biology , cytoskeleton , microbiology and biotechnology , biochemistry , chemistry , computational biology , enzyme , cell
Cortactin is a cytoskeletal protein which increases the metastasis of cancer cells. Cortactin is commonly located and over‐expressed in cancer cells. Because of its role in cancer, we sought to better understand the structure of cortactin. Our analysis involved expression of cortactin from E. coli , purification using His‐tag and ion exchange column purification, dialysis, and analysis by SDS‐PAGE. Previous work in the laboratory suggested that ion exchange purification resulted in the isolation of folding variants of cortactin. To understand the structures of these folding variants, we used the apoptotic enzymes calpain and caspase to probe solvent exposed regions of the protein and analyze the resulting protein fragments by SDS‐PAGE. There are three putative caspase sites on cortactin (at the N‐terminus, middle, and C‐terminus) and several putative calpain sites distributed throughout the structure. In the future, we plan on further analyzing cortactin by digging deeper into its conformation through other chemical analysis. Support or Funding Information This work is supported by the College of Saint Scholastica SSC Summer Research Fellowships. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .