A previously unobserved conformation for the human Pex5p receptor suggests roles for intrinsic flexibility and rigid domain motions in ligand binding.

ABSTRACT:

Background

The C-terminal tetratricopeptide (TPR) repeat domain of Pex5p recognises proteins carrying a peroxisomal targeting signal type 1 (PTS1) tripeptide in their C-terminus. Previously, structural data have been obtained from the TPR domain of Pex5p in both the liganded and unliganded states, indicating a conformational change taking place upon cargo protein binding. Such a conformational change would be expected to play a major role both during PTS1 protein recognition as well as in cargo release into the peroxisomal lumen. However, little information is available on the factors that may regulate such structural changes.

Results

We have used a range of biophysical and computational methods to further analyse the conformational flexibility and ligand binding of Pex5p. A

SUBMITTER: Stanley WA 

PROVIDER: S-EPMC1854907 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature