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PMID: 16616874 Published · ppublish English Comparative Study Journal Article Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural Review

Membrane binding domains.

Biochimica et biophysica acta ·Vol. 1761 ·No. 8 ·2006-08-00 ·Pages 805-11

Hurley JH

Abstract

Eukaryotic signaling and trafficking proteins are rich in modular domains that bind cell membranes. These binding events are tightly regulated in space and time. The structural, biochemical, and biophysical mechanisms for targeting have been worked out for many families of membrane binding domains. This review takes a comparative view of seven major classes of membrane binding domains, the C1, C2, PH, FYVE, PX, ENTH, and BAR domains. These domains use a combination of specific headgroup interactions, hydrophobic membrane penetration, electrostatic surface interactions, and shape complementarity to bind to specific subcellular membranes.

MeSH Terms
Animals Binding Sites/physiology Cell Membrane/metabolism Humans Hydrophobic and Hydrophilic Interactions Lipid Metabolism Membrane Lipids/metabolism Models, Molecular Protein Structure, Tertiary Protein Transport Signal Transduction
Chemicals
Membrane Lipids
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Hurley James H
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, USA. hurley@helix.nih.gov
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Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
2006-08-00
Epub
2006-00-24
Pages
805-11
Language
English
Region
Netherlands
NLM ID
0217513
PMCID
PMC2049088
Subset
IM
Grants
Intramural NIH HHS · Z01 DK036118-14 · United States
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