6GSE

Solution structure of the capsid domain from the activity-regulated cytoskeleton-associated protein, Arc

Summary for 6GSE

• Entry DOI: 10.2210/pdb6gse/pdb
• NMR Information: BMRB: 34285
• Descriptor: Activity-regulated cytoskeleton-associated protein (1 entity in total)
• Functional Keywords: retroviral capsid domain, nmda receptor interaction, gag protein, protein binding
• Biological source: Rattus norvegicus (Norway Rat)
• Total number of polymer chains: 1
• Total formula weight: 18996.31

Authors

Nielsen, L.D.,Erlendsson, S.,Teilum, K. (deposition date: 2018-06-14, release date: 2019-05-22, Last modification date: 2024-06-19)

Primary citation

Nielsen, L.D.,Pedersen, C.P.,Erlendsson, S.,Teilum, K.
The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor.
Structure, 27:1071-1081.e5, 2019

PubMed Abstract: The activity-regulated cytoskeleton-associated protein, Arc, is highly expressed in neuronal dendrites and is involved in synaptic scaling and plasticity. Arc exhibits homology to the capsid-forming Gag proteins from retroviruses and can encapsulate its own mRNA and transport it to neighboring neurons. However, the molecular events that lead to the assembly of Arc capsids and how the capsid formation is regulated are not known. Here we show that the capsid domain of Arc may transiently form homogeneous oligomers of similar size as capsids formed by full-length Arc. We determined a high-resolution structure of the monomeric Arc capsid domain and mapped the initial structural change in the oligomerization process to the N-terminal part of the capsid domain. Peptide ligands from the NMDA receptor subunits inhibit oligomerization, which suggests that Arc's ability to transfer mRNA between cells may be regulated by protein-protein interactions at the synapse.

PubMed: 31080121
DOI: 10.1016/j.str.2019.04.001

Experimental method

SOLUTION NMR
SOLUTION SCATTERING