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Article

Domain structure and lipid interaction in human apolipoproteins A-I and E, a general model.

The Journal of biological chemistry - 27 Jun 2003

Saito Hiroyuki, Dhanasekaran Padmaja, Nguyen David, Holvoet Paul, Lund-Katz Sissel, Phillips Michael C

Abstract excerpt

Detailed structural information on human exchangeable apolipoproteins (apo) is required to understand their functions in lipid transport. Using a series of deletion mutants that progressively lacked different regions along the molecule, we probed the structural organization of lipid-free human apoA-I and the role of different domains in lipid binding, making comparisons to apoE, which is a member of the same gene...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 12709430
DOI: 10.1074/jbc.M303365200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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