7ZM5

Structure of Mossman virus receptor binding protein

Summary for 7ZM5

• Entry DOI: 10.2210/pdb7zm5/pdb
• Descriptor: Attachment glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: attachment glycoprotein, glycoprotein, receptor binding protein, viral protein
• Biological source: Mossman narmovirus
• Total number of polymer chains: 2
• Total formula weight: 140844.32

Authors

Stelfox, A.J.,Bowden, T.A.,Rissanen, I.,Harlos, K. (deposition date: 2022-04-19, release date: 2023-09-13, Last modification date: 2024-11-06)

Primary citation

Stelfox, A.J.,Oguntuyo, K.Y.,Rissanen, I.,Harlos, K.,Rambo, R.,Lee, B.,Bowden, T.A.
Crystal structure and solution state of the C-terminal head region of the narmovirus receptor binding protein.
Mbio, 14:e0139123-e0139123, 2023

PubMed Abstract: Genetically diverse paramyxoviruses are united in their presentation of a receptor-binding protein (RBP), which works in concert with the fusion protein to facilitate host-cell entry. The C-terminal head region of the paramyxoviral RBP, a primary determinant of host-cell tropism and inter-species transmission potential, forms structurally distinct classes dependent upon protein and glycan receptor specificity. Here, we reveal the architecture of the C-terminal head region of the RBPs from Nariva virus (NarV) and Mossman virus (MosV), two archetypal rodent-borne paramyxoviruses within the recently established genus , family . Our analysis reveals that while narmoviruses retain the general architectural features associated with paramyxoviral RBPs, namely, a six-bladed β-propeller fold, they lack the structural motifs associated with known receptor-mediated host-cell entry pathways. This investigation indicates that the RBPs of narmoviruses exhibit pathobiological features that are distinct from those of other paramyxoviruses.

PubMed: 37737607
DOI: 10.1128/mbio.01391-23

Experimental method

X-RAY DIFFRACTION (1.62 Å)