Crystal structure of designed PX domain from cytokine-independent survival kinase and implications on evolution-based protein engineering.

ABSTRACT: The Phox homology domain (PX domain) is a phosphoinositide-binding structural domain that is critical in mediating protein and cell membrane association and has been found in more than 100 eukaryotic proteins. The abundance of PX domains in nature offers an opportunity to redesign the protein using EvoDesign, a computational approach to design new sequences based on structure profiles of multiple evolutionarily related proteins. In this study, we report the X-ray crystallographic structure of a designed PX domain from the cytokine-independent survival kinase (CISK), which has been implicated as functioning in parallel with PKB/Akt in cell survival and insulin responses. Detailed data analysis of the designed CISK-PX protein demonstrates positive impacts of knowledge-based secondary structu

SUBMITTER: Shultis D 

PROVIDER: S-EPMC4520749 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature