Structural properties of target binding by profilaggrin A and B domains and other S100 fused-type calcium-binding proteins.

ABSTRACT:

Background

Profilaggrin belongs to the S100 fused-type protein family expressed in keratinocytes and is important for skin barrier integrity. Its N-terminus contains an S100 ("A") domain and a unique "B" domain with a nuclear localization sequence.

Objective

To determine whether profilaggrin B domain cooperates with the S100 domain to bind macromolecules. To characterize the biochemical and structural properties of the profilaggrin N-terminal "AB" domain and compare it to other S100 fused-type proteins.

Methods

We used biochemical (protease protection, light scattering, fluorescence spectroscopy, pull-down assays) and computational techniques (sequence analysis, molecular modeling with crystallographic structures) to examine human profilaggrin and S100 fused-type prot

SUBMITTER: Hinbest AJ 

PROVIDER: S-EPMC7752840 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature