Structural and energetic determinants of tyrosylprotein sulfotransferase sulfation specificity.

ABSTRACT:

Motivation

Tyrosine sulfation is a type of post-translational modification (PTM) catalyzed by tyrosylprotein sulfotransferases (TPST). The modification plays a crucial role in mediating protein-protein interactions in many biologically important processes. There is no well-defined sequence motif for TPST sulfation, and the underlying determinants of TPST sulfation specificity remains elusive. Here, we perform molecular modeling to uncover the structural and energetic determinants of TPST sulfation specificity.

Results

We estimate the binding affinities between TPST and peptides around tyrosines of both sulfated and non-sulfated proteins to differentiate them. We find that better differentiation is achieved after including energy costs associated with local unfolding of the t

SUBMITTER: Nedumpully-Govindan P 

PROVIDER: S-EPMC4155453 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature