Stabilization of the Hinge Region of Human E-selectin Enhances Binding Affinity to Ligands Under Force.

ABSTRACT:

Introduction

E-selectin is a member of the selectin family of cell adhesion molecules expressed on the plasma membrane of inflamed endothelium and facilitates initial leukocyte tethering and subsequent cell rolling during the early stages of the inflammatory response via binding to glycoproteins expressing sialyl Lewis^X and sialyl Lewis^A (sLe^X/A). Existing crystal structures of the extracellular lectin/EGF-like domain of E-selectin complexed with sLe^X have revealed that E-selectin can exist in two conformation states, a low affinity (bent) conformation, and a high affinity (extended) conformation. The differentiating characteristic of the two conformations is the interdomain angle between the lectin and the EGF-like domain.

Meth

SUBMITTER: Cao TM 

PROVIDER: S-EPMC7878631 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature