Major
Biology
Access Type
Open Access
Abstract
Phosducin-like proteins (PhLPs) are a subclass of the thioredoxin (Trx) superfamily of proteins. The CryoEM structure of the chaperonin TriC/CCT complexed with PhLP2A supports the hypothesis that PhLPs are involved in the folding of cytoskeletal proteins, actin, and tubulin. However, the precise function of PhLP is not well understood. Several members of the Trx family of proteins are redox active and act as chaperones to assist protein folding. Additionally, the amino acid sequence alignment between TXNDC9 and PhLP2A reveals the redox-active cysteine to be conserved. We hypothesize that PhLP2A, like its structural homolog TXNDC9, is redox active.
Faculty Mentors & Instructors
Dr. Stefan Kanzok, PhD, Biology ; Samantha Webster, graduate student mentor, Biology
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Investigating The Enzymatic Redox Activity of Human Phosducin-Like Protein 2A
Phosducin-like proteins (PhLPs) are a subclass of the thioredoxin (Trx) superfamily of proteins. The CryoEM structure of the chaperonin TriC/CCT complexed with PhLP2A supports the hypothesis that PhLPs are involved in the folding of cytoskeletal proteins, actin, and tubulin. However, the precise function of PhLP is not well understood. Several members of the Trx family of proteins are redox active and act as chaperones to assist protein folding. Additionally, the amino acid sequence alignment between TXNDC9 and PhLP2A reveals the redox-active cysteine to be conserved. We hypothesize that PhLP2A, like its structural homolog TXNDC9, is redox active.