2RND
Structure of the N-terminal BARpeptide in DPC micelles
Summary for 2RND
| Entry DOI | 10.2210/pdb2rnd/pdb |
| Related | 2rmy |
| NMR Information | BMRB: 11049 |
| Descriptor | Myc box-dependent-interacting protein 1 (1 entity in total) |
| Functional Keywords | barpeptide, micelle, nmr-structure, alternative splicing, anti-oncogene, cell cycle, coiled coil, cytoplasm, developmental protein, differentiation, disease mutation, endocytosis, host-virus interaction, nucleus, phosphoprotein, sh3 domain |
| Biological source | Homo sapiens (Human) |
| Cellular location | Isoform BIN1: Nucleus. Isoform IIA: Cytoplasm: O00499 |
| Total number of polymer chains | 1 |
| Total formula weight | 3714.42 |
| Authors | Loew, C.,Weininger, U.,Balbach, J. (deposition date: 2007-12-16, release date: 2008-10-14, Last modification date: 2024-05-29) |
| Primary citation | Low, C.,Weininger, U.,Lee, H.,Schweimer, K.,Neundorf, I.,Beck-Sickinger, A.G.,Pastor, R.W.,Balbach, J. Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers Biophys.J., 95:4315-4323, 2008 Cited by PubMed Abstract: Bin/Amphiphysin/Rvs-homology (BAR) domains generate and sense membrane curvature by binding the negatively charged membrane to their positively charged concave surfaces. N-BAR domains contain an N-terminal extension (helix-0) predicted to form an amphipathic helix upon membrane binding. We determined the NMR structure and nano-to-picosecond dynamics of helix-0 of the human Bin1/Amphiphysin II BAR domain in sodium dodecyl sulfate and dodecylphosphocholine micelles. Molecular dynamics simulations of this 34-amino acid peptide revealed electrostatic and hydrophobic interactions with the detergent molecules that induce helical structure formation from residues 8-10 toward the C-terminus. The orientation in the micelles was experimentally confirmed by backbone amide proton exchange. The simulation and the experiment indicated that the N-terminal region is disordered, and the peptide curves to adopted the micelle shape. Deletion of helix-0 reduced tubulation of liposomes by the BAR domain, whereas the helix-0 peptide itself was fusogenic. These findings support models for membrane curving by BAR domains in which helix-0 increases the binding affinity to the membrane and enhances curvature generation. PubMed: 18658220DOI: 10.1529/biophysj.108.134155 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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