Native-like environments afford novel mechanistic insights into membrane proteins Editorial


Authors: Notti, R. Q.; Walz, T.
Title: Native-like environments afford novel mechanistic insights into membrane proteins
Abstract: Advances in cryogenic electron microscopy (cryo-EM) enabled routine near-atomic structure determination of membrane proteins, while nanodisc technology has provided a way to provide membrane proteins with a native or native-like lipid environment. After giving a brief history of membrane mimetics, we present example structures of membrane proteins in nanodiscs that revealed information not provided by structures obtained in detergent. We describe how the lipid environment surrounding the membrane protein can be custom designed during nanodisc assembly and how it can be modified after assembly to test functional hypotheses. Because nanodiscs most closely replicate the physiologic environment of membrane proteins and often afford novel mechanistic insights, we propose that nanodiscs ought to become the standard for structural studies on membrane proteins. © 2022 Elsevier Ltd
Keywords: amphiphilic copolymers; membrane scaffold proteins; native nanodiscs; single-particle cryo-electron microscopy
Journal Title: Trends in Biochemical Sciences
Volume: 47
Issue: 7
ISSN: 0968-0004
Publisher: Elsevier Inc.  
Date Published: 2022-07-01
Start Page: 561
End Page: 569
Language: English
DOI: 10.1016/j.tibs.2022.02.008
PUBMED: 35331611
PROVIDER: scopus
DOI/URL:
Notes: Review -- Export Date: 1 June 2022 -- Source: Scopus
Altmetric
Citation Impact
BMJ Impact Analytics
MSK Authors
  1. Ryan Quin Notti
    4 Notti