Journal article

The cryo-EM structure of the endocytic receptor DEC-205

Benjamin S Gully, Hariprasad Venugopal, Alex J Fulcher, Zhihui Fu, Jessica Li, Felix A Deuss, Carmen Llerena, William R Heath, Mireille H Lahoud, Irina Caminschi, Jamie Rossjohn, Richard Berry

JOURNAL OF BIOLOGICAL CHEMISTRY | ELSEVIER | Published : 2021

Abstract

DEC-205 (CD205), a member of the macrophage mannose receptor protein family, is the prototypic endocytic receptor of dendritic cells, whose ligands include phosphorothioated cytosine-guanosine oligonucleotides, a motif often seen in bacterial or viral DNA. However, despite growing biological and clinical significance, little is known about the structural arrangement of this receptor or any of its family members. Here, we describe the 3.2 Å cryo-EM structure of human DEC-205, thereby illuminating the structure of the mannose receptor protein family. The DEC-205 monomer forms a compact structure comprising two intercalated rings of C-type lectin-like domains, where the N-terminal cysteine-rich..

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Grants

Awarded by Australian Research Council


Awarded by National Health and Medical Research Council (NHMRC)


Awarded by ARC Laureate Fellowship


Awarded by NHMRC


Funding Acknowledgements

This work was supported by the Monash University Ramaciotti Centre for Cryo-Electron Microscopy, the Monash MASSIVE high-performance computing facility, and the Monash MicroImaging facility. This work was supported by the Australian Research Council (CE140100011), National Health and Medical Research Council (NHMRC) (1113293). J. R. is supported by an ARC Laureate Fellowship (FL160100049). R. B. was supported by a Career Development Fellowship from the NHMRC (APP1109901).