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A Consensus Model of Human Apolipoprotein A-I in its Monomeric and Lipid-free State
- Source :
- Nature structural & molecular biology
- Publication Year :
- 2017
-
Abstract
- Apolipoprotein (apo)A-I is an organizing scaffold protein that is critical to high-density lipoprotein (HDL) structure and metabolism, probably mediating many of its cardioprotective properties. However, HDL biogenesis is poorly understood, as lipid-free apoA-I has been notoriously resistant to high-resolution structural study. Published models from low-resolution techniques share certain features but vary considerably in shape and secondary structure. To tackle this central issue in lipoprotein biology, we assembled a team of structural biologists specializing in apolipoproteins and set out to build a consensus model of monomeric lipid-free human apoA-I. Combining novel and published cross-link constraints, small-angle X-ray scattering (SAXS), hydrogen-deuterium exchange (HDX) and crystallography data, we propose a time-averaged model consistent with much of the experimental data published over the last 40 years. The model provides a long-sought platform for understanding and testing details of HDL biogenesis, structure and function.
- Subjects :
- 0301 basic medicine
Scaffold protein
Models, Molecular
Cardiotonic Agents
Apolipoprotein B
Computational biology
Crystallography, X-Ray
Article
Protein Structure, Secondary
oligomerization
03 medical and health sciences
Protein structure
Structural Biology
Humans
Consensus model
Computer Simulation
structure
Molecular Biology
Protein secondary structure
mass spectrometry
biology
Apolipoprotein A-I
Chemistry
Human apolipoprotein
030104 developmental biology
Biochemistry
biology.protein
lipids (amino acids, peptides, and proteins)
Lipoproteins, HDL
lipid-free
Biogenesis
Lipoprotein
cross-linking
Subjects
Details
- Language :
- English
- ISSN :
- 15459985 and 15459993
- Volume :
- 24
- Issue :
- 12
- Database :
- OpenAIRE
- Journal :
- Nature structural & molecular biology
- Accession number :
- edsair.doi.dedup.....971d1883688f7b742ea1c25b9f110c42