Double and triple thermodynamic mutant cycles reveal the basis for specific MsbA-lipid interactions

Double and triple thermodynamic mutant cycles reveal the basis for specific MsbA-lipid interactions

Structural and functional studies of the ATP-binding cassette transporter MsbA have revealed two distinct lipopolysaccharide (LPS) binding sites: one located in the central cavity and the other at a membrane-facing, exterior site. Although these binding sites are known to be important for MsbA funct...

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Bibliographic Details
Main Authors: Jixing Lyu, Tianqi Zhang, Michael T Marty, David Clemmer, David H Russell, Arthur Laganowsky
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2024-01-01
Series:eLife
Subjects:
protein-lipid interactions
native mass spectrometry
ABC transporter
thermodynamics
Online Access:https://elifesciences.org/articles/91094

Internet

https://elifesciences.org/articles/91094

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