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Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-a...

Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-a...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1685044233

Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-association

About this item

Full title

Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-association

Publisher

United States: Public Library of Science

Journal title

PLoS computational biology, 2015-03, Vol.11 (3), p.e1004148-e1004148

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

Substantial evidence in support of the formation of opioid receptor (OR) di-/oligomers suggests previously unknown mechanisms used by these proteins to exert their biological functions. In an attempt to guide experimental assessment of the identity of the minimal signaling unit for ORs, we conducted extensive coarse-grained (CG) molecular dynamics...

Alternative Titles

Full title

Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-association

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1685044233

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1685044233

Other Identifiers

ISSN

1553-7358,1553-734X

E-ISSN

1553-7358

DOI

10.1371/journal.pcbi.1004148

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