Structural Perspectives on Extracellular Recognition and Conformational Changes of Several Type-I Transmembrane Receptors.

ABSTRACT: Type-I transmembrane proteins represent a large group of 1,412 proteins in humans with a multitude of functions in cells and tissues. They are characterized by an extracellular, or luminal, N-terminus followed by a single transmembrane helix and a cytosolic C-terminus. The domain composition and structures of the extracellular and intercellular segments differ substantially amongst its members. Most of the type-I transmembrane proteins have roles in cell signaling processes, as ligands or receptors, and in cellular adhesion. The extracellular segment often determines specificity and can control signaling and adhesion. Here we focus on recent structural understanding on how the extracellular segments of several diverse type-I transmembrane proteins engage in interactions and can undergo con

SUBMITTER: Chataigner LMP 

PROVIDER: S-EPMC7427315 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature