6gse
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of the capsid domain from the activity-regulated cytoskeleton-associated protein, Arc== | |
| + | <StructureSection load='6gse' size='340' side='right'caption='[[6gse]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6gse]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GSE FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gse OCA], [http://pdbe.org/6gse PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gse RCSB], [http://www.ebi.ac.uk/pdbsum/6gse PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gse ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ARC_RAT ARC_RAT]] Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the stress fiber dynamics and cell migration (By similarity). Required for consolidation of synaptic plasticity as well as formation of long-term memory. Regulates endocytosis of AMPA receptors in response to synaptic activity. Required for homeostatic synaptic scaling of AMPA receptors.<ref>PMID:17088212</ref> <ref>PMID:17088213</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor.,Nielsen LD, Pedersen CP, Erlendsson S, Teilum K Structure. 2019 Apr 16. pii: S0969-2126(19)30123-6. doi:, 10.1016/j.str.2019.04.001. PMID:31080121<ref>PMID:31080121</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6gse" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Erlendsson, S]] | ||
| + | [[Category: Nielsen, L D]] | ||
| + | [[Category: Teilum, K]] | ||
| + | [[Category: Gag protein]] | ||
| + | [[Category: Nmda receptor interaction]] | ||
| + | [[Category: Protein binding]] | ||
| + | [[Category: Retroviral capsid domain]] | ||
Revision as of 06:46, 23 May 2019
Solution structure of the capsid domain from the activity-regulated cytoskeleton-associated protein, Arc
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