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Updated: Jun 19, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Crystal structures of all-alpha type membrane proteins.
Karen McLuskey1, Aleksander W Roszak, Yanshi Zhu
1Westchem, Department of Chemistry, Glasgow Biomedical Research Centre, University of Glasgow, 120 University Place, Glasgow, G12 8TA, UK. k.mcluskey@chem.gla.ac.uk
This review details all-alpha type membrane protein structures determined by X-ray crystallography. These insights advance understanding of integral membrane protein function and structure-function relationships.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Integral membrane proteins perform vital biological functions.
- Understanding their 3D structures is key to elucidating function.
- All-alpha type membrane proteins represent a functionally diverse class.
Purpose of the Study:
- To review and describe the structures of all-alpha type membrane proteins.
- To highlight the contributions of these structures to understanding membrane protein function.
- To provide an overview of structures determined via X-ray crystallography.
Main Methods:
- X-ray crystallography was used to determine protein structures.
- A comprehensive review of existing structural data was conducted.
- Individual protein systems and their structures were described.
Main Results:
- The review covers numerous all-alpha type membrane protein structures.
- Structural data provides insights into individual protein functions.
- Structure-function relationships in membrane proteins are elucidated.
Conclusions:
- The determined structures of all-alpha type membrane proteins are crucial for understanding their roles.
- These structural studies offer deep insights into biological systems.
- Advances in structural biology enhance knowledge of integral membrane protein function.
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