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Cited by 77Cellular transport and secretionProtein Structure and DynamicsLipid Membrane Structure and Behavior

The Crystal Structure of the BAR Domain from Human Bin1/Amphiphysin II and Its Implications for Molecular Recognition

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Casal, Eva, Federici, Luca, Zhang, Wei, Fernandez-Recio, Juan, Priego, Eva-Maria, Miguel, Ricardo Nuñez, DuHadaway, James B., Prendergast, George C. +2 more·2006·Biochemistry
DOI 10.1021/bi060717kPMC PMC2572078
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Abstract

BAR domains are found in proteins that bind and remodel membranes and participate in cytoskeletal and nuclear processes. Here, we report the crystal structure of the BAR domain from the human Bin1 protein at 2.0 A resolution. Both the quaternary and tertiary architectures of the homodimeric Bin1BAR domain are built upon "knobs-into-holes" packing of side chains, like those found in conventional left-handed coiled-coils, and this packing governs the curvature of a putative membrane-engaging concave face. Our calculations indicate that the Bin1BAR domain contains two potential sites for protein-protein interactions on the convex face of the dimer. Comparative analysis of structural features reveals that at least three architectural subtypes of the BAR domain are encoded in the human genome, represented by the Arfaptin, Bin1/Amphiphysin, and IRSp53 BAR domains. We discuss how these principal groups may differ in their potential to form regulatory heterotypic interactions.

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Authors
Casal, E., Federici, L., Zhang, W., Fernandez-Recio, J., Priego, E.-M., Miguel, R. N., DuHadaway, J. B., Prendergast, G. C., Luisi, B. F., & Laue, E. D.
Affiliations
  • Lankenau Institute for Medical Research (US)
  • Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, U.K., Ce.S.I. Centro Studi sull'Invecchiamento and Dipartimento di Scienze Biomediche, Università di Chieti “G. D'Annunzio”, Via dei Vestini 31, 66013 Chieti, Italy, Institute of Biomedical Research, Barcelona Science Park, Josep Samitier 1-5, 08028 Barcelona, Spain, and Lankenau Institute for Medical Research, 100 Lancaster Avenue, Wynnewood, Pennsylvania 19096
ORCID
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2006-10-01
Volume
45
Issue
43
Pages
12917-12928
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi060717k
PMC
PMC2572078
OpenAlex
W2086012791
Cited by
77
References
3
Citations by year
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FWCI
2.62
Type
journal article
Language
en
Open access
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • Wellcome Trust
  • European Synchrotron Radiation Facility
  • National Cancer Institute (R01CA100123)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Keywords
BAR domain, BIN1, crystal structure, homodimer, membrane curvature, membrane binding, protein-protein interaction, IRSp53, heterotypic interactions, membrane remodeling
MeSH terms
Animals, Binding Sites, Crystallization, Humans, Models, Molecular, Nuclear Proteins, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Protein Structure, Quaternary, Tumor Suppressor Proteins, Structural Homology, Protein, Adaptor Proteins, Signal Transducing

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