ErbB1-4 are members of the human epidermal growth factor receptor (EGFR) family of tyrosine kinases. ErbB2 has been implicated in many different types of cancer,most notably breast cancer. Structural studies reveal that ErbB2 and the Drosophila EGFR (DER) share significant similarity. DER is known to be inhibited by Kekkon 1, a transmembrane leucine-rich repeat immunoglobulin, or LIG protein. To investigate the mechanism of binding to DER and determine if Kek1 could bind ErbB2, an enzyme-linked extracellular interaction screen (ELEXIS) was utilized.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Scott, Victoria Ashley

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-050116-233027

Advisor

• Duffy, Joseph B.

Year

• 2016

Date created

• 2016-05-01

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright